2.4.1.109: dolichyl-phosphate-mannose-protein mannosyltransferase
This is an abbreviated version!
For detailed information about dolichyl-phosphate-mannose-protein mannosyltransferase, go to the full flat file.
Word Map on EC 2.4.1.109
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2.4.1.109
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muscular
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dystrophy
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o-mannosylation
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walker-warburg
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alpha-dystroglycan
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pomgnt1
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o-glycosylation
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fukutin
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muscle-eye-brain
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dystroglycanopathies
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dystroglycan
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girdle
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alpha-dystroglycanopathy
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lissencephaly
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fukuyama
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hypoglycosylation
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limb-girdle
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alpha-dg
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pomts
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cobblestone
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heterotopia
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fukutin-related
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medicine
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gmppb
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o-mannose
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agriculture
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diagnostics
- 2.4.1.109
- muscular
- dystrophy
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o-mannosylation
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walker-warburg
- alpha-dystroglycan
- pomgnt1
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o-glycosylation
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fukutin
- muscle-eye-brain
- dystroglycanopathies
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dystroglycan
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girdle
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alpha-dystroglycanopathy
- lissencephaly
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fukuyama
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hypoglycosylation
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limb-girdle
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alpha-dg
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pomts
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cobblestone
- heterotopia
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fukutin-related
- medicine
- gmppb
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o-mannose
- agriculture
- diagnostics
Reaction
Synonyms
AapmtA, AfPmt1p, AnPmtA, AnPmtB, AnPmtC, dolichol phosphomannose-protein mannosyltransferase, dolichyl phosphate-mannose:protein O-mannosyltransferase, dolichyl-phosphate-mannose--protein mannosyltransferase 1, dolichyl-phosphate-mannose--protein mannosyltransferase 2, dolichyl-phosphate-mannose--protein mannosyltransferase 4, dolichyl-phosphate-mannose-protein mannosyltransferase, dolichyl-phosphate-mannose-protein mannosyltransferase 1, dolichyl-phosphate-mannose-protein mannosyltransferase 2, Drosophila O-mannosyltransferase Rotated Abdomen, Drosophila O-mannosyltransferase Twisted, HpPmt1p, mannosyltransferase, dolichol phosphomannose-protein, More, O-glycoside mannosyltransferase, O-mannosyltransferase, O-mannosyltransferase 1, ogm1, ogm2, ogm4, Oma1, Oma2, Oma4, Omg1, Omg2, Omg4, PMT, PMT1, Pmt1 O-mannosyltransferase, Pmt1A, Pmt1D, Pmt1p, Pmt1p-Pmt2p, PMT2, Pmt2A, Pmt2D, Pmt2p, PMT3, PMT4, Pmt4A, Pmt4D, Pmt4p, PMT5, Pmt5p, Pmt6, PMT7, PmtA, pmtB, pmtC, PMTI, POMT1, POMT2, protein mannosyltransferase, protein O-D-mannosyltransferase, protein O-mannosyl-transferase 1, protein O-mannosyl-transferase 2, protein O-mannosyltransferase, protein O-mannosyltransferase 1, protein O-mannosyltransferase 2, protein O-mannosyltransferase A, protein O-mannosyltransferase Pmt4, protein O-mannosyltransferases 1, protein O-mannosyltransferases 2, protein-O-mannosyltransferase-1, protein-Omannosyltransferase, RT, sPOMT2, tPOmt2, TW, Um05433, Um10749, Um11220
ECTree
2.4.1.109 dolichyl-phosphate-mannose-protein mannosyltransferaseAdvanced search results
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results (Engineering
Engineering on EC 2.4.1.109 - dolichyl-phosphate-mannose-protein mannosyltransferase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
yes
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mutants lacking or overexpressing one of the two or both O-mannosyltransferases Rotated Abdomen and Twisted show that both are required for in vivo production of high molecular mass dystroglycan, overexpression of only one isoform does not increase its amount over wild-type, lack of either one of the isoforms or both isoforms lacking double mutant do not produce the high molecular mass dystroglycan
D77A/E78A
D77A/E78A/D92A/E93A
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the PMT1/PMT2 mutant shows 0.24% activity compared to the wild type enzyme
D80E/E81D
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the PMT4 mutant shows 116.54% activity compared to the wild type enzyme
D92A/E93A
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the PMT2 mutant shows 3.63% activity compared to the wild type enzyme
L171A
stable enzyme with reduced activity causing phenotype limb girdle muscular dystrophy 2K, together with partial heterozygous deletion p.A589VfsX38 mutant, reduced amounts of O-mannosyl linked glyco-epitope (IIH6) on alpha-dystroglycans resulting in less than 100-125 kDa alpha-dystroglycans, about 40% residual enzyme activity
N16Q
N16Q/N435Q/N471Q/N539Q
N330Q
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2-3 kDa smaller than wild-type corresponding to single N-glycan chain, single mutation with no effect on activity
N435Q
N445Q
N471Q
N528Q
N539Q
N583Q
N98Q
N98Q/N330Q/N445Q/N528Q/N583Q
D96A
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site-directed mutagenesis, exchange of conserved residue in the central loop, reduced activity
E78A
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site-directed mutagenesis, exchange of conserved residue in the central loop, highly reduced activity
H346A/H348A
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site-directed mutagenesis, exchange of conserved residue in the central loop, reduced activity
H411A
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site-directed mutagenesis, exchange of conserved residue in the central loop, slightly reduced activity
H472A
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site-directed mutagenesis, exchange of conserved residue in the central loop, reduced activity
K234A
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site-directed mutagenesis, exchange of conserved residue in the central loop, slightly reduced activity
L399A
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site-directed mutagenesis, exchange of conserved residue in the central loop, reduced activity
L408A
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site-directed mutagenesis, exchange of conserved residue in the central loop, highly reduced activity
L408A/H411A
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site-directed mutagenesis, exchange of conserved residue in the central loop, highly reduced activity
N370A
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site-directed mutagenesis, exchange of conserved residue in the central loop, slightly reduced activity
Q359A/Q360A
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site-directed mutagenesis, exchange of conserved residue in the central loop, reduced activity
Q493A/E495A
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site-directed mutagenesis, exchange of conserved residue in the central loop, reduced activity
R138A
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site-directed mutagenesis, exchange of conserved residue in the central loop, highly reduced activity
R398A
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site-directed mutagenesis, exchange of conserved residue in the central loop, reduced activity
R469A
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site-directed mutagenesis, exchange of conserved residue in the central loop, slightly reduced activity
R64 A
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site-directed mutagenesis, exchange of conserved residue in the central loop, highly reduced activity
W253A
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site-directed mutagenesis, exchange of conserved residue in the central loop, slightly reduced activity
additional information
D77A/E78A
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the PMT1 mutant shows 0.19% activity compared to the wild type enzyme
D77A/E78A
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the PMT1 mutant shows 3.59% activity compared to the wild type enzyme
N16Q
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not smaller than wild-type, may be too close to membrane for a glycosylation site, single mutation with about 70% of wild-type activity
N16Q/N435Q/N471Q/N539Q
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together with POMT2 mutant N98Q/N330Q/N445Q/N528Q/N583Q, significantly lower activity than double wild-type, a lack of glycosylation prevents solubilization
N16Q/N435Q/N471Q/N539Q
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together with wild-type POMT2, significantly lower activity than double wild-type, a lack of glycosylation prevents solubilization
N435Q
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2-3 kDa smaller than wild-type corresponding to single N-glycan chain, single mutation with about 70% of wild-type activity
N445Q
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2-3 kDa smaller than wild-type corresponding to single N-glycan chain, single mutation with no effect on activity
N471Q
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2-3 kDa smaller than wild-type corresponding to single N-glycan chain, single mutation with about 70% of wild-type activity
N528Q
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2-3 kDa smaller than wild-type corresponding to single N-glycan chain, single mutation with no effect on activity
N539Q
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2-3 kDa smaller than wild-type corresponding to single N-glycan chain, single mutation with no effect on activity
N583Q
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2-3 kDa smaller than wild-type corresponding to single N-glycan chain, single mutation with no effect on activity
N98Q
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2-3 kDa smaller than wild-type corresponding to single N-glycan chain, single mutation with about 50% of wild-type activity
N98Q/N330Q/N445Q/N528Q/N583Q
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together with POMT1 mutant N16Q/N435Q/N471Q/N539Q, significantly lower activity than double wild-type, a lack of glycosylation prevents solubilization
N98Q/N330Q/N445Q/N528Q/N583Q
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together with wild-type POMT1, significantly lower activity than double wild-type, a lack of glycosylation prevents solubilization
additional information
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enzyme disruption mutant, 6% of wild-type activity, underglycosylation of an extracellular glucoamylase. Disruption mutant shows abnormal cell morphology and alteration in carbohydrate composition, reduction n the skeletal polysaccharides in the cell wall
additional information
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Anpmta + AnpmtB double disruptant is viable but very slow growing with morphological characteristics (swollen hyphae with ballon structures + hyperbranched hyphae) cumulative of single disruptants at 30 and 42°C, partial improvement of defects by addition of osmotic stabilizer
additional information
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AnpmtA disruptant, increased sensitivity to hygromycin B (increased cell wall permeability), glycoprotetin profile (plasma membrane proteins) almost indistinguishable from wild-type, underglycosylation of protein AN5660 upon AnpmtC diruption
additional information
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AnPmtB disruptant shows wild-type colony formation at 30°C, slightly repressed growth at 42°C, the osmotic stabilizer 0.6 M KCl reduces these effects, conidiation reduced to about 56%, swollen vesicles, hyperbranching of hyphae (defect in polarity maintenance), underglycosylation of glucoamylase I upon gene disruption, higher sensitivity to inhibitors of cell wall synthesis (beta-glucan and beta-1,3-glucan production) congo red and micafungin, not to calcofluor (inhibiting chitin synthesis), no increased sensitivity to hygromycin B, glycoproetin profile (plasma membrane proteins) almost indistinguishable from wild-type, underglycosylation of glucoamylase I upon AnpmtB diruption
additional information
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AnpmtC disruptant with highest growth repression, swollen, frequently branched hyphae, strongly reduced conidia formation (6% of wild-type), recovery of hyphal structures in the presence of osmotic stabilizers (0.6 M KCl, 0.8 M NaCl, or 1.2 M sorbitol) at 42°C, enables conidiophore and conidia production (abnormal and fewer), underglycosylation of glucoamylase I upon gene diruption, higher sensitivity to inhibitors of cell wall synthesis (beta-glucan and beta-1,3-glucan production) congo red and micafungin, not to calcofluor (inhibiting chitin synthesis), more sensitive to hygromycin B than wild-type, increase of 65 kDa proteins, of mannose-containing glycoproteins (plasma membrane proteins) of about 80 kDa, reduced number of proteins larger than 100 kDa and of 75 kDa, underglycosylation of glucoamylase I and of protein AN5660 upon AnpmtC diruption
additional information
at 25 and 30°C normal growth of single deletion mutants, reduced growth at high temperatures (37 and 42°C), deltapmtA deletion mutant is more heat sensitive than deltapmtC and deltapmtB, double deletion mutant deltapmtA + deltapmtB is the most heat sensitive, partial restoration of heat tolerance by addition of the osmotic sorbitol, the pmtA deletion mutant is more sensitive to cell wall-perturbing agents Calcofluor and Congo red than the wild-type, at 30°C more germ tubes emerge early compared to wild-type and the other deletion mutants except double deletion mutant deltapmtA + deltapmtB, swollen conidia, partial or no conidiogenous layers, at 42°C 2 to 3times swollen conidia, no germ tubes, fewer conidia
additional information
at 25 and 30°C normal growth of single deletion mutants, reduced growth at high temperatures (37 and 42°C), deltapmtA deletion mutant is more heat sensitive than deltapmtC and deltapmtB, double deletion mutant deltapmtA + deltapmtB is the most heat sensitive, partial restoration of heat tolerance by addition of the osmotic sorbitol, the pmtA deletion mutant is more sensitive to cell wall-perturbing agents Calcofluor and Congo red than the wild-type, at 30°C more germ tubes emerge early compared to wild-type and the other deletion mutants except double deletion mutant deltapmtA + deltapmtB, swollen conidia, partial or no conidiogenous layers, at 42°C 2 to 3times swollen conidia, no germ tubes, fewer conidia
additional information
at 25 and 30°C normal growth of single deletion mutants, reduced growth at high temperatures (37 and 42°C), deltapmtA deletion mutant is more heat sensitive than deltapmtC and deltapmtB, double deletion mutant deltapmtA + deltapmtB is the most heat sensitive, partial restoration of heat tolerance by addition of the osmotic sorbitol, the pmtA deletion mutant is more sensitive to cell wall-perturbing agents Calcofluor and Congo red than the wild-type, at 30°C more germ tubes emerge early compared to wild-type and the other deletion mutants except double deletion mutant deltapmtA + deltapmtB, swollen conidia, partial or no conidiogenous layers, at 42°C 2 to 3times swollen conidia, no germ tubes, fewer conidia
additional information
at 25 and 30°C normal growth of single deletion mutants, reduced growth at high temperatures (37 and 42°C), double deletion mutant deltapmtA + deltapmtB is the most heat sensitive, deltapmtA deletion mutant is more heat sensitive than deltapmtC and deltapmtB, partial restoration of heat tolerance by addition of the osmotic sorbitol or KCl (not conidial production), the deltapmtC deletion mutant is resistant to Calcofluor at all temperatures but sensitive to Congo red at elevated temperatures, at 30°C more multiple germ tubes than in the wild-type and in the other deletion mutants, excessive aerial hyphae, fewer conidiophores on elongated stalks, condigiogenous layers misplaced, at 37°C vesicles and conidiogenous layers swollen, fewer spores at all temperatures at 42°C swollen germ tubes and hyperbranching
additional information
at 25 and 30°C normal growth of single deletion mutants, reduced growth at high temperatures (37 and 42°C), double deletion mutant deltapmtA + deltapmtB is the most heat sensitive, deltapmtA deletion mutant is more heat sensitive than deltapmtC and deltapmtB, partial restoration of heat tolerance by addition of the osmotic sorbitol or KCl (not conidial production), the deltapmtC deletion mutant is resistant to Calcofluor at all temperatures but sensitive to Congo red at elevated temperatures, at 30°C more multiple germ tubes than in the wild-type and in the other deletion mutants, excessive aerial hyphae, fewer conidiophores on elongated stalks, condigiogenous layers misplaced, at 37°C vesicles and conidiogenous layers swollen, fewer spores at all temperatures at 42°C swollen germ tubes and hyperbranching
additional information
at 25 and 30°C normal growth of single deletion mutants, reduced growth at high temperatures (37 and 42°C), double deletion mutant deltapmtA + deltapmtB is the most heat sensitive, deltapmtA deletion mutant is more heat sensitive than deltapmtC and deltapmtB, partial restoration of heat tolerance by addition of the osmotic sorbitol or KCl (not conidial production), the deltapmtC deletion mutant is resistant to Calcofluor at all temperatures but sensitive to Congo red at elevated temperatures, at 30°C more multiple germ tubes than in the wild-type and in the other deletion mutants, excessive aerial hyphae, fewer conidiophores on elongated stalks, condigiogenous layers misplaced, at 37°C vesicles and conidiogenous layers swollen, fewer spores at all temperatures at 42°C swollen germ tubes and hyperbranching
additional information
at 25 and 30°C normal growth of single deletion mutants, reduced growth at high temperatures (37 and 42°C), pmtA deletion mutant is more heat sensitive than deltapmtC and deltapmtB, double deletion mutant deltapmtA + deltapmtB is the most heat sensitive, partial restoration of heat tolerance by addition of the osmotic sorbitol or KCl, at 25°C the pmtB deletion mutant grows as well as the wild-type in the presence of cell wall-perturbing agents, at 30 and 37°C it is hypersensitive to Calcofluor, at 42°C it is resistant to Calcofluor, to Congo red it is hypersensitive at 37 and 42°C, resistant at lower temperatures, at 42°C lysis of 30% of hyphen tips, at permissive temperature mostly normal conidiophores, occasional lysed vesicles, at restrictive temperature many swollen conidiophore stalks and lysed vesicles, fewer conidia, at 30°C hyphae are growing from adjacent compartments into lysed areas forming intrahyphal hyphae
additional information
at 25 and 30°C normal growth of single deletion mutants, reduced growth at high temperatures (37 and 42°C), pmtA deletion mutant is more heat sensitive than deltapmtC and deltapmtB, double deletion mutant deltapmtA + deltapmtB is the most heat sensitive, partial restoration of heat tolerance by addition of the osmotic sorbitol or KCl, at 25°C the pmtB deletion mutant grows as well as the wild-type in the presence of cell wall-perturbing agents, at 30 and 37°C it is hypersensitive to Calcofluor, at 42°C it is resistant to Calcofluor, to Congo red it is hypersensitive at 37 and 42°C, resistant at lower temperatures, at 42°C lysis of 30% of hyphen tips, at permissive temperature mostly normal conidiophores, occasional lysed vesicles, at restrictive temperature many swollen conidiophore stalks and lysed vesicles, fewer conidia, at 30°C hyphae are growing from adjacent compartments into lysed areas forming intrahyphal hyphae
additional information
at 25 and 30°C normal growth of single deletion mutants, reduced growth at high temperatures (37 and 42°C), pmtA deletion mutant is more heat sensitive than deltapmtC and deltapmtB, double deletion mutant deltapmtA + deltapmtB is the most heat sensitive, partial restoration of heat tolerance by addition of the osmotic sorbitol or KCl, at 25°C the pmtB deletion mutant grows as well as the wild-type in the presence of cell wall-perturbing agents, at 30 and 37°C it is hypersensitive to Calcofluor, at 42°C it is resistant to Calcofluor, to Congo red it is hypersensitive at 37 and 42°C, resistant at lower temperatures, at 42°C lysis of 30% of hyphen tips, at permissive temperature mostly normal conidiophores, occasional lysed vesicles, at restrictive temperature many swollen conidiophore stalks and lysed vesicles, fewer conidia, at 30°C hyphae are growing from adjacent compartments into lysed areas forming intrahyphal hyphae
additional information
double deletion mutant of pmtA + pmtB is the only viable double mutant, it shows slightly retarded growth even at 25°C and is the most heat sensitive deletion mutant, followed in sensitivity by deltapmtA, deltapmtC, and deltapmtB, partial restoration of heat tolerance by addition of the osmotic sorbitol or KCl (not conidial production), the double deletion mutant is more sensitive to cell wall-perturbing agents Calcofluor and Congo red than the wild-type at all tested temperatures, at 25°C swollen conidiophore stalks, vesicles, and conidiogenous layers, at 30°C more germ tubes emerge early compared to wild-type and the other deletion mutants except deltapmtA, lysis of hyphen tips at permissive temperature, at 37°C vegetative and aerial hyphae badly swollen, conidiophores not detectable, reduced conidia productiondefective polar growth at restrictive temperature, at 30°C hyphae are growing from adjacent compartments into lysed areas forming intrahyphal hyphae
additional information
double deletion mutant of pmtA + pmtB is the only viable double mutant, it shows slightly retarded growth even at 25°C and is the most heat sensitive deletion mutant, followed in sensitivity by deltapmtA, deltapmtC, and deltapmtB, partial restoration of heat tolerance by addition of the osmotic sorbitol or KCl (not conidial production), the double deletion mutant is more sensitive to cell wall-perturbing agents Calcofluor and Congo red than the wild-type at all tested temperatures, at 25°C swollen conidiophore stalks, vesicles, and conidiogenous layers, at 30°C more germ tubes emerge early compared to wild-type and the other deletion mutants except deltapmtA, lysis of hyphen tips at permissive temperature, at 37°C vegetative and aerial hyphae badly swollen, conidiophores not detectable, reduced conidia productiondefective polar growth at restrictive temperature, at 30°C hyphae are growing from adjacent compartments into lysed areas forming intrahyphal hyphae
additional information
double deletion mutant of pmtA + pmtB is the only viable double mutant, it shows slightly retarded growth even at 25°C and is the most heat sensitive deletion mutant, followed in sensitivity by deltapmtA, deltapmtC, and deltapmtB, partial restoration of heat tolerance by addition of the osmotic sorbitol or KCl (not conidial production), the double deletion mutant is more sensitive to cell wall-perturbing agents Calcofluor and Congo red than the wild-type at all tested temperatures, at 25°C swollen conidiophore stalks, vesicles, and conidiogenous layers, at 30°C more germ tubes emerge early compared to wild-type and the other deletion mutants except deltapmtA, lysis of hyphen tips at permissive temperature, at 37°C vegetative and aerial hyphae badly swollen, conidiophores not detectable, reduced conidia productiondefective polar growth at restrictive temperature, at 30°C hyphae are growing from adjacent compartments into lysed areas forming intrahyphal hyphae
additional information
double deletion mutant of pmtB + pmtC is not viable
additional information
double deletion mutant of pmtB + pmtC is not viable
additional information
double deletion mutant of pmtB + pmtC is not viable
additional information
double deletion mutants of pmtA + pmtC is not viable
additional information
double deletion mutants of pmtA + pmtC is not viable
additional information
double deletion mutants of pmtA + pmtC is not viable
additional information
the triple deletion mutant of pmtA + pmtB + pmtC is not viable
additional information
the triple deletion mutant of pmtA + pmtB + pmtC is not viable
additional information
the triple deletion mutant of pmtA + pmtB + pmtC is not viable
additional information
generation of a truncated mutant lacking the C-terminal Pmt1 MIR-containing region (Pmt1DELTA311-902) by targeted gene replacement and construction of the C-terminal Pmt1 MIR-containing region deletion strains and complementation strains. Construction and analysis of the C-terminal Pmt1 MIR-containing region-affected transcriptomes. Complementation by expression of wild-type enzyme. The mutant shows altered conidial yield, conidial germination, hydrophobicity and adhesion, phenotypes, overview
additional information
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generation of a truncated mutant lacking the C-terminal Pmt1 MIR-containing region (Pmt1DELTA311-902) by targeted gene replacement and construction of the C-terminal Pmt1 MIR-containing region deletion strains and complementation strains. Construction and analysis of the C-terminal Pmt1 MIR-containing region-affected transcriptomes. Complementation by expression of wild-type enzyme. The mutant shows altered conidial yield, conidial germination, hydrophobicity and adhesion, phenotypes, overview
additional information
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generation of a truncated mutant lacking the C-terminal Pmt1 MIR-containing region (Pmt1DELTA311-902) by targeted gene replacement and construction of the C-terminal Pmt1 MIR-containing region deletion strains and complementation strains. Construction and analysis of the C-terminal Pmt1 MIR-containing region-affected transcriptomes. Complementation by expression of wild-type enzyme. The mutant shows altered conidial yield, conidial germination, hydrophobicity and adhesion, phenotypes, overview
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additional information
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disruption after amino acid D439 results in pmt1A lacking mutants are viable but show distinct defects in cell morphology and cell integrity (wild-type comparable growth at 30°C, reduced growth at 37°C, no growth at 39°C in contrast to wild-type, more susceptible to SDS medium, enlarged cells subject to spontaneous lysis, attenuated virulence), Pmt1/Pmt4 double mutants are not viable, pmt1A mutant is susceptible to sorbitol (2.5 M) and to 0.1% SDS, reduced survival upon macrophage attack
additional information
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disruption after amino acid E468 results in pmt2A lacking mutants, not viable, one wild-type allele is necessary for growth, after sporulation no haploid pmt2 lacking mutants are found, Pmt2 is essential but an intact Pmt2 gene lacking the other two isoforms is not sufficient for viability, may be due to interaction with the other isoforms
additional information
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disruption after amino acid K461 results in pmt4A lacking mutants, viable but with distinct defects in cell morphology and cell integrity (wild-type comparable growth at 30°C, reduced growth at 37°C, no growth at 39°C in contrast to wild-type, poor growth on high salt medium, abnormal septum formation, enlarged cells subject to spontaneous lysis, multi-cell aggregate formation based on defects in cell separation, delayed melanin production, slightly reduced capsule size, attenuated virulence), Pmt1/Pmt4 double mutants are not viable, points to necessary interaction with the Pmt2 isoform or essential combined target, the pmt4A mutant is susceptible to sorbitol (2 M), reduced survival upon macrophage attack
additional information
disruption after amino acid N508 results in pmt2D lacking mutants, not viable, one wild-type allele is necessary for growth, after sporulation no haploid pmt2 lacking mutants are found, Pmt2 is essential but an intact Pmt2 gene lacking the other two isoforms is not sufficient for viability may be due to interaction with the other isoforms
additional information
disruption after amino acid N508 results in pmt2D lacking mutants, not viable, one wild-type allele is necessary for growth, after sporulation no haploid pmt2 lacking mutants are found, Pmt2 is essential but an intact Pmt2 gene lacking the other two isoforms is not sufficient for viability may be due to interaction with the other isoforms
additional information
disruption after amino acid N508 results in pmt2D lacking mutants, not viable, one wild-type allele is necessary for growth, after sporulation no haploid pmt2 lacking mutants are found, Pmt2 is essential but an intact Pmt2 gene lacking the other two isoforms is not sufficient for viability may be due to interaction with the other isoforms
additional information
disruption after amino acid Q412 results in pmt4D lacking mutants, aviable but with distinct defects in cell morphology and cell integrity (wild-type comparable growth at 30°C, reduced growth at 37°C, no growth at 39°C in contrast to wild-type, poor growth on high salt medium, abnormal septum formation, enlarged cells subject to spontaneous lysis, multi-cell aggregate formation based on defects in cell separation, delayed melanin production, slightly reduced capsule size, attenuated virulence), Pmt1/Pmt4 double mutants are not viable, points to necessary interaction with the Pmt2 isoform or essential combined target, the pmt4D strain is not inhibited by sorbitol but is inhibited by SDS, bilateral crossing of two pmt4D mutant strains delays mating reaction with reduced filament formation, less aerial hyphae, irregular shape and thickness of filaments with swollen distal tips
additional information
disruption after amino acid Q412 results in pmt4D lacking mutants, aviable but with distinct defects in cell morphology and cell integrity (wild-type comparable growth at 30°C, reduced growth at 37°C, no growth at 39°C in contrast to wild-type, poor growth on high salt medium, abnormal septum formation, enlarged cells subject to spontaneous lysis, multi-cell aggregate formation based on defects in cell separation, delayed melanin production, slightly reduced capsule size, attenuated virulence), Pmt1/Pmt4 double mutants are not viable, points to necessary interaction with the Pmt2 isoform or essential combined target, the pmt4D strain is not inhibited by sorbitol but is inhibited by SDS, bilateral crossing of two pmt4D mutant strains delays mating reaction with reduced filament formation, less aerial hyphae, irregular shape and thickness of filaments with swollen distal tips
additional information
disruption after amino acid Q412 results in pmt4D lacking mutants, aviable but with distinct defects in cell morphology and cell integrity (wild-type comparable growth at 30°C, reduced growth at 37°C, no growth at 39°C in contrast to wild-type, poor growth on high salt medium, abnormal septum formation, enlarged cells subject to spontaneous lysis, multi-cell aggregate formation based on defects in cell separation, delayed melanin production, slightly reduced capsule size, attenuated virulence), Pmt1/Pmt4 double mutants are not viable, points to necessary interaction with the Pmt2 isoform or essential combined target, the pmt4D strain is not inhibited by sorbitol but is inhibited by SDS, bilateral crossing of two pmt4D mutant strains delays mating reaction with reduced filament formation, less aerial hyphae, irregular shape and thickness of filaments with swollen distal tips
additional information
disruption after amino acid W315 results in pmt1D lacking mutants are viable but show distinct defects in cell morphology and cell integrity (wild-type comparable growth at 30°C, reduced growth at 37°C, no growth at 39°C in contrast to wild-type, more susceptible to SDS medium, enlarged cells subject to spontaneous lysis, attenuated virulence), Pmt1/Pmt4 double mutants are not viable, the pmt1D mutant grows poorly in sorbitol, is unaffected by SDS, no defects in mating and crossing are observed
additional information
disruption after amino acid W315 results in pmt1D lacking mutants are viable but show distinct defects in cell morphology and cell integrity (wild-type comparable growth at 30°C, reduced growth at 37°C, no growth at 39°C in contrast to wild-type, more susceptible to SDS medium, enlarged cells subject to spontaneous lysis, attenuated virulence), Pmt1/Pmt4 double mutants are not viable, the pmt1D mutant grows poorly in sorbitol, is unaffected by SDS, no defects in mating and crossing are observed
additional information
disruption after amino acid W315 results in pmt1D lacking mutants are viable but show distinct defects in cell morphology and cell integrity (wild-type comparable growth at 30°C, reduced growth at 37°C, no growth at 39°C in contrast to wild-type, more susceptible to SDS medium, enlarged cells subject to spontaneous lysis, attenuated virulence), Pmt1/Pmt4 double mutants are not viable, the pmt1D mutant grows poorly in sorbitol, is unaffected by SDS, no defects in mating and crossing are observed
additional information
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mutants lacking or overexpressing one of the two or both O-mannosyltransferases Rotated Abdomen and Twisted show that both are required for in vivo production of high molecular mass dystroglycan, overexpression of only one isoform does not increase its amount over wild-type, lack of either one of the isoforms or both isoforms lacking double mutant do not produce the high molecular mass dystroglycan
additional information
heterozygous deletion leading to a frame shift mutation causing an amino acid exchange A589V and a premature stop codon after 38 amino acids (p.A589VfsX38), reduced enzyme stability, reduced amounts of O-mannosyl linked glyco-epitope (IIH6) on alpha-dystroglycans resulting in less than 100-125 kDa alpha-dystroglycans, about 40% residual enzyme activity, phenotype limb girdle muscular dystrophy 2K
additional information
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heterozygous deletion leading to a frame shift mutation causing an amino acid exchange A589V and a premature stop codon after 38 amino acids (p.A589VfsX38), reduced enzyme stability, reduced amounts of O-mannosyl linked glyco-epitope (IIH6) on alpha-dystroglycans resulting in less than 100-125 kDa alpha-dystroglycans, about 40% residual enzyme activity, phenotype limb girdle muscular dystrophy 2K
additional information
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single site mutations defective in potential glycosylation sites do not change enzyme activity, mutaions of all such sites cause a loss of enzyme activity, probably due to decreased hydrophilicity
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single site mutations defective in potential glycosylation sites do not change enzyme activity, mutations of all such sites cause a loss of enzyme activity, probably du to decreased hydrophilicity
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mutations of all N-glycosylation sites of either isoform POMT1 or POMT2 cause a loss of enzyme activity
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construction of Pichia pastoris single and all PMT knockout mutant strains, the DELTApmt1 and DELTApmt2 strains secrete protein with significantly reduced O-glycan site occupancy
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construction of Pichia pastoris single and all PMT knockout mutant strains, the DELTApmt1 and DELTApmt2 strains secrete protein with significantly reduced O-glycan site occupancy
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construction of Pichia pastoris single and all PMT knockout mutant strains, the DELTApmt1 and DELTApmt2 strains secrete protein with significantly reduced O-glycan site occupancy
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construction of diverse deletion mutants of PMT1, effect on activity and complex formation with PMT2, overview
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homozygous diploid double disruption mutants of PMT1 and PMT2 lead to reduced enzyme activity and a severe defect in sporulation, lethal phenotype when combined with a disruption mutation in dolichyl-phosphate-mannose-glycolipid alpha-mannosyltransferase, EC 2.4.1.130, genes
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homozygous diploid double disruption mutants of PMT1 and PMT2 lead to reduced enzyme activity and a severe defect in sporulation, lethal phenotype when combined with a disruption mutation in dolichyl-phosphate-mannose-glycolipid alpha-mannosyltransferase, EC 2.4.1.130, genes
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homozygous diploid double disruption mutants of PMT1 and PMT2 lead to reduced enzyme activity and a severe defect in sporulation, lethal phenotype when combined with a disruption mutation in dolichyl-phosphate-mannose-glycolipid alpha-mannosyltransferase, EC 2.4.1.130, genes
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construction of all single, double and triple mutants of the genes PMT1-4 by gene disruption and crosses, characterization concerning growth, morphology, and their sensitivity to killer toxin K1, sorbitol dependence, caffeine and calcofluor white, overview
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construction of all single, double and triple mutants of the genes PMT1-4 by gene disruption and crosses, characterization concerning growth, morphology, and their sensitivity to killer toxin K1, sorbitol dependence, caffeine and calcofluor white, overview
additional information
construction of all single, double and triple mutants of the genes PMT1-4 by gene disruption and crosses, characterization concerning growth, morphology, and their sensitivity to killer toxin K1, sorbitol dependence, caffeine and calcofluor white, overview
additional information
construction of all single, double and triple mutants of the genes PMT1-4 by gene disruption and crosses, characterization concerning growth, morphology, and their sensitivity to killer toxin K1, sorbitol dependence, caffeine and calcofluor white, overview
additional information
construction of all single, double and triple mutants of the genes PMT1-4 by gene disruption and crosses, characterization concerning growth, morphology, and their sensitivity to killer toxin K1, sorbitol dependence, caffeine and calcofluor white, overview
additional information
construction of all single, double and triple mutants of the genes PMT1-4 by gene disruption and crosses, characterization concerning growth, morphology, and their sensitivity to killer toxin K1, sorbitol dependence, caffeine and calcofluor white, overview
additional information
construction of all single, double and triple mutants of the genes PMT1-4 by gene disruption and crosses, characterization concerning growth, morphology, and their sensitivity to killer toxin K1, sorbitol dependence, caffeine and calcofluor white, overview
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PMT1 null mutant shows increased heat lability, alpa-D-mannose transfer only to serine residue of the substrate peptide Ac-YNPTSV-NH2, not to threonine and valine like with the wild-type
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PMT2 disruption mutant shows reduced in vitro and in vivo activity
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PMT2 disruption mutant shows reduced in vitro and in vivo activity
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PMT1 and PMT2 double disruption mutant shows severe growth defect but retain residual activity due to an additional enzyme
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PMT1 and PMT2 double disruption mutant shows severe growth defect but retain residual activity due to an additional enzyme
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PMT3 and 4 gene disruption does not alter enzyme activity
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PMT3 and 4 gene disruption does not alter enzyme activity
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PMT3 and 4 gene disruption does not alter enzyme activity
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construction of defective mutants of PMT1-4,6, determination of substrate specificities
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PMT2 haploid mutants grow slightly slower than the wild-type, the enzyme is required but not essential for normal vegetative growth of the cells
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PMT2 haploid mutants grow slightly slower than the wild-type, the enzyme is required but not essential for normal vegetative growth of the cells
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complementation studies with Schizosaccharomyces pombe deletion mutants show that pmt1 is a functional homolog
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complementation studies with Schizosaccharomyces pombe deletion mutants show that pmt4 is a functional homolog
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pmt4 and pmt1 and double deletion mutants are viable with normal growth rates and mating, normal disease symptoms are developed in infected Zea mays
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the single deletion mutant of pmt1 is viable with normal growth rates and mating, causes disease development in Zea may comparable to wild-type, no increased sensitivity to antifungal substances such as congo red, chlorpromazine, calcofluor white, and caffein or to thermal stress (34 and 36°C), oxidative stress (H2O2), osmotic stress (SDS and sorbitol), or salt-based stress (NaCl, CaCl2)
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the single deletion mutant of pmt4 is viable with normal growth rates and mating, causes no disease symptoms in Zea mays, not even in plants infected via the stigma, no increased sensitivity to antifungal substances such as congo red, chlorpromazine, calcofluor white, and caffein or to thermal stress (34 and 36°C), to oxidative stress (H2O2), to osmotic stress by sorbitol but to SDS, or to salt-based stress (NaCl, CaCl2), no changed activity of secreted hydrolytic enzymes (cellulase, pectinase, amylase activity), normal filament formation but lower appressorium formation and aberrant appressorium formation, hyphae are built close to the plant surface but do not intrude the epidermal cell layer, inhibition of the defensive plant reactive oxygen species formation does not restore virulence
