2.1.1.287: 25S rRNA (adenine645-N1)-methyltransferase
This is an abbreviated version!
For detailed information about 25S rRNA (adenine645-N1)-methyltransferase, go to the full flat file.
Reaction
Synonyms
25S rRNA m1A645 methyltransferase, 5S rRNA (adenine(645)-N(1))-methyltransferase, CaRRP8, ribosomal RNA-processing protein 8, Rrp8
ECTree
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General Information
General Information on EC 2.1.1.287 - 25S rRNA (adenine645-N1)-methyltransferase
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evolution
malfunction
physiological function
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the N1-methyladenosine in helix 25.1 of 25/28S rRNA seems to be highly conserved
evolution
the N1-methyladenosine in helix 25.1 of 25/28S rRNA seems to be highly conserved
evolution
the N1-methyladenosine in helix 25.1 of 25/28S rRNA seems to be highly conserved
evolution
Candida albicans CBS 356
-
the N1-methyladenosine in helix 25.1 of 25/28S rRNA seems to be highly conserved
-
evolution
-
the N1-methyladenosine in helix 25.1 of 25/28S rRNA seems to be highly conserved
-
evolution
-
the N1-methyladenosine in helix 25.1 of 25/28S rRNA seems to be highly conserved
-
evolution
-
the N1-methyladenosine in helix 25.1 of 25/28S rRNA seems to be highly conserved
-
evolution
-
the N1-methyladenosine in helix 25.1 of 25/28S rRNA seems to be highly conserved
-
Loss of m1A645 in yeast alters the rRNA topology by affecting eL32 interaction with 25S rRNA. Methylation of the N1 atom of adenosine leads to a net positive charge on the base and is expected to disrupt the canonical Watson-Crick base pairing. The loss of m1A645 leads to structural changes in and around the helix 25.1 region of the 25S rRNA and causes formation of stalled preinitiation complex called halfmers. Loss of m1A645 does not influence the conformation of helix 7 and 60S synthesis. But 60S lacking m1A645 are less competent to bind to 40S subunits and therefore cause the formation of halfmers in the absence of m1A645. Loss of m1A645 in yeast alters the rRNA topology by affecting eL32 interaction with 25S rRNA. Loss of Rrp8 leads to an accumulation of the aberrant 21S pre-rRNA due to defects in A2 cleavage and to cold sensitivity for growth. Both of these phenotypes are fully complemented by Candida albicans CaRRP8, whereas the expression of Schizosaccharomyces pombe SpRRP8 cannot restore 21S accumulation defects and cold sensitivity. The human nucleomethylin (NML or RRP8) fails to complement the pre-rRNA processing phenotype and the growth cold sensitivity of DELTArrp8
malfunction
-
Loss of m1A645 in yeast alters the rRNA topology by affecting eL32 interaction with 25S rRNA. Methylation of the N1 atom of adenosine leads to a net positive charge on the base and is expected to disrupt the canonical Watson-Crick base pairing. The loss of m1A645 leads to structural changes in and around the helix 25.1 region of the 25S rRNA and causes formation of stalled preinitiation complex called halfmers. Loss of m1A645 does not influence the conformation of helix 7 and 60S synthesis. But 60S lacking m1A645 are less competent to bind to 40S subunits and therefore cause the formation of halfmers in the absence of m1A645. Loss of m1A645 in yeast alters the rRNA topology by affecting eL32 interaction with 25S rRNA. Loss of Rrp8 leads to an accumulation of the aberrant 21S pre-rRNA due to defects in A2 cleavage and to cold sensitivity for growth. Both of these phenotypes are fully complemented by Candida albicans CaRRP8, whereas the expression of Schizosaccharomyces pombe SpRRP8 cannot restore 21S accumulation defects and cold sensitivity. The human nucleomethylin (NML or RRP8) fails to complement the pre-rRNA processing phenotype and the growth cold sensitivity of DELTArrp8
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the enzyme is important for ribosome biogenesis
physiological function
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the enzyme CaRRP8 from Candida albicans can fully complement the Saccharomyces cerevisiae rrp8 deficient mutant phenotype, i.e. accumulation of the aberrant 21S pre-rRNA due to defects in A2 cleavage and to cold sensitivity for growth
physiological function
the expression of Schizosaccharomyces pombe SpRRP8 cannot restore 21S accumulation defects and cold sensitivity in of Saccharomyces cerevisiae DELTArrp8 mutant strain
physiological function
Candida albicans CBS 356
-
the enzyme CaRRP8 from Candida albicans can fully complement the Saccharomyces cerevisiae rrp8 deficient mutant phenotype, i.e. accumulation of the aberrant 21S pre-rRNA due to defects in A2 cleavage and to cold sensitivity for growth
-
physiological function
-
the expression of Schizosaccharomyces pombe SpRRP8 cannot restore 21S accumulation defects and cold sensitivity in of Saccharomyces cerevisiae DELTArrp8 mutant strain
-
physiological function
-
the expression of Schizosaccharomyces pombe SpRRP8 cannot restore 21S accumulation defects and cold sensitivity in of Saccharomyces cerevisiae DELTArrp8 mutant strain
-
physiological function
-
the enzyme CaRRP8 from Candida albicans can fully complement the Saccharomyces cerevisiae rrp8 deficient mutant phenotype, i.e. accumulation of the aberrant 21S pre-rRNA due to defects in A2 cleavage and to cold sensitivity for growth
-