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evolution
PMT family members are conserved throughout the fungal and animal kingdoms. They are further subdivided into the PMT1, PMT2, and PMT4 subfamilies, which include transferases closely related to Saccharomyces cerevisiae Pmt1p, Pmt2p, and Pmt4p, respectively. In fungi, at least one member of each subfamily is present, whereas in animals only PMT2 and PMT4 subfamily members are conserved. In Saccharomyces, Pmt1p, Pmt2p, and Pmt4p account for the major transferase activities although at least six PMTs (Pmt1p-Pmt6p) are present
evolution
the enzyme is a member of the protein-O-mannosyltransferase (PMT) family. Pichia pastoris has five PMT genes. Based on sequence homology, the PMTs can be grouped into three subfamilies, with both PMT1 and PMT2 subfamilies possessing two members each (PMT1 and PMT5, and PMT2 and PMT6, respectively). The remaining subfamily, PMT4, has only one member, PMT4. PMT1 and PMT2 each play a significant role in O-glycosylation
evolution
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the enzyme is a member of the protein-O-mannosyltransferase (PMT) family. Pichia pastoris has five PMT genes. Based on sequence homology, the PMTs can be grouped into three subfamilies, with both PMT1 and PMT2 subfamilies possessing two members each (PMT1 and PMT5, and PMT2 and PMT6, respectively). The remaining subfamily, PMT4, has only one member, PMT4. PMT1 and PMT2 each play a significant role in O-glycosylation
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malfunction
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AnpmtA + AnpmtB double disruptant is viable but slow growing with morphological characteristics cumulative of single disruptants
malfunction
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AnpmtA + AnpmtB double disruptant is viable but slow growing with morphological characteristics cumulative of single disruptants, hyperglycosylation of specific target proteins
malfunction
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AnpmtB disruptant shows wild-type colony formation at 30°C, slightly repressed growth at 42°C, conidiation reduced to about 50%, hyperbranching of hyphae (defect in polarity maintenance)
malfunction
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defects in O-mannosylation are associated with muscular dystrophies (dystroglycanopathies)
malfunction
dystroglycanopathies (muscular dystrophy due to abnormal glycosylation of alpha-dystroglycan) such as the severe Walker-Warburg syndrome (brain and eye abnormalities, mild limb girdle muscular dystrophy)
malfunction
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loss of the O-mannosyltransferase is associated with a reduced formation frequency of the invasive structure, the appressorium, combined with a loss in the ability to penetrate the plant cuticle
malfunction
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mutation in either one of the complex forming enzymes can lead to Walker-Warburg syndrome, a congenital muscular dystrophy with abnormal neuronal migration
malfunction
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pmt4 deletion mutant with strong reduction in appressorium formation, the few formed appressoria lack the capacity to penetrate the plant cuticle, reduced pathogenicity, no effects on vegetative growth or mating, normal polar growth of infectious hyphae
malfunction
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pmtC disruptant with highest growth repression, swollen, frequently branched hyphae, no conidia formation, recovery of hyphal structures in the presence of osmotic stabilizers, enables conidiophore and conidia production (abnormal and fewer) at 42°C
malfunction
single enzyme deletion mutants are viable, at elevated temperatures they show cell wall-associated defects and increased sensitivity to cell wall-perturbing agents, and defects in developmental patterning, partial restoration of wild-type growth with the osmotic sorbitol
malfunction
virulence of the human fungal pathogen causing meningoencephalitis depends on extracellular factors including the O-glycosylation of proteins
malfunction
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virulence of the human fungal pathogen causing meningoencephalitis depends on extracellular factors including the O-glycosylation of proteins
malfunction
PMT2 knockout, and to a lesser extent a PMT1 knockout, in addition to a reduction in O-glycan site occupancy also leads to shortened O-glycan chain lengths
malfunction
the lack of C-terminal Pmt1 MIR-containing region affects transcriptomes, altering the transcription of genes involved in asexual development, e.g. transcription patterns of seven conidiation-associated genes flbA-flbD, fluG, hyd1, and hyd2. Loss of the enzyme's C-terminal Pmt1 MIR-containing region affects mannosylation of the cell wall proteins. The Pmt1DELTA311-902 cells show significant increases in lectin binding when probed with either the ConA or the JAL lectins as compared with the wild-type strain. Increased binding of the WGA lectin is also detected or Pmt1delta311-902 cells, but no obvious difference in reactivity with GNL between the wild-type and Pmt1delta311-902 cells. The mutant shows altered conidial yield, conidial germination, hydrophobicity and adhesion. Phenotypes, overview. Hyphal bodies isolated from insects infected with Pmt1DELTA311-902 cells are elongated and significantly longer than their wild-type counterparts. In addition, hyphal branching is seen in numerous cells, a phenomenon rarely detected in wild-type (and complemented strain) samples
malfunction
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PMT2 knockout, and to a lesser extent a PMT1 knockout, in addition to a reduction in O-glycan site occupancy also leads to shortened O-glycan chain lengths
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malfunction
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the lack of C-terminal Pmt1 MIR-containing region affects transcriptomes, altering the transcription of genes involved in asexual development, e.g. transcription patterns of seven conidiation-associated genes flbA-flbD, fluG, hyd1, and hyd2. Loss of the enzyme's C-terminal Pmt1 MIR-containing region affects mannosylation of the cell wall proteins. The Pmt1DELTA311-902 cells show significant increases in lectin binding when probed with either the ConA or the JAL lectins as compared with the wild-type strain. Increased binding of the WGA lectin is also detected or Pmt1delta311-902 cells, but no obvious difference in reactivity with GNL between the wild-type and Pmt1delta311-902 cells. The mutant shows altered conidial yield, conidial germination, hydrophobicity and adhesion. Phenotypes, overview. Hyphal bodies isolated from insects infected with Pmt1DELTA311-902 cells are elongated and significantly longer than their wild-type counterparts. In addition, hyphal branching is seen in numerous cells, a phenomenon rarely detected in wild-type (and complemented strain) samples
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metabolism
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a complex of protein O-mannosyltransferase 1 and 2 catalyzes the initial step of O-mannosyl glycan biosynthesis
metabolism
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isoforms POMT1 and POMT2 catalyze the initial step of O-mannosyl glycan biosynthesis
metabolism
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protein O-mannosyltransferase 1 (POMT1) and its homolog, POMT2, are responsible for the catalysis of the first step in O-mannosyl glycan synthesis
physiological function
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AnpmtB, hyphal development and differentiation, polarity maintenance
physiological function
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AnpmtC, hyphal development and differentiation, maintenance of cell wall integrity
physiological function
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fungal morphology and conidia formation
physiological function
O-glycosylation of proteins
physiological function
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O-glycosylation of proteins
physiological function
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O-mannosylation can modulate the ligand-binding activity of alpha-dystroglycan
physiological function
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O-mannosylation is essential for virulence of the fungus
physiological function
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pmt4 is important for pathogenesis (appressorium formation and penetration)
physiological function
role in cell wall integrity pathway and developmental patterning by providing spatial cues
physiological function
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the Pmt1p-Pmt2p complex participates in endoplasmic reticulum protein quality control. The Pmt1p-Pmt2p complex is required for the fast endoplasmic reticulum exit of wild-type substrate Gas1p
physiological function
Dol-P-beta-Man:protein alpha-mannosyltransferases are initiating the essential protein O-mannosylation of secretory and membrane proteins in the endoplasmic reticulum. Pmt1p-loop1 is crucial for cross-linking of the photoreactive peptide
physiological function
protein O-mannosylation in fungi is initiated at the endoplasmic reticulum by a family of protein-O-mannosyltransferases that transfer mannose from dolichyl phosphate-activated mannose to serine or threonine residues of proteins entering the endoplasmic reticulum
physiological function
the C-terminal Pmt1 MIR-containing region affects transcriptomes. Requirement of the C-terminal Pmt1 MIR containing region on Pmt1 O-mannosyltransferase enzyme activity in vivo. The C-terminal MIR-containing domain of Pmt1 is involved in cell wall integrity, cell surface characteristics, and cell adhesion. But the Pmt1 C-terminus domain containing the MIR motifs is dispensable for fungal virulence
physiological function
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protein O-mannosylation in fungi is initiated at the endoplasmic reticulum by a family of protein-O-mannosyltransferases that transfer mannose from dolichyl phosphate-activated mannose to serine or threonine residues of proteins entering the endoplasmic reticulum
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physiological function
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the C-terminal Pmt1 MIR-containing region affects transcriptomes. Requirement of the C-terminal Pmt1 MIR containing region on Pmt1 O-mannosyltransferase enzyme activity in vivo. The C-terminal MIR-containing domain of Pmt1 is involved in cell wall integrity, cell surface characteristics, and cell adhesion. But the Pmt1 C-terminus domain containing the MIR motifs is dispensable for fungal virulence
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additional information
cell wall composition of wild-type strain and the Pmt1DELTA311-902 mutant strain, overview
additional information
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cell wall composition of wild-type strain and the Pmt1DELTA311-902 mutant strain, overview
additional information
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cell wall composition of wild-type strain and the Pmt1DELTA311-902 mutant strain, overview
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