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Information on EC 2.1.1.309 - 18S rRNA (guanine1575-N7)-methyltransferase and Organism(s) Homo sapiens and UniProt Accession O43709

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IUBMB Comments
The enzyme, found in eukaryotes, is involved in pre-rRNA processing. The numbering corresponds to the enzyme from the yeast Saccharomyces cerevisiae .
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This record set is specific for:
Homo sapiens
UNIPROT: O43709
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The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Synonyms
wbscr22, bud23, wbscr22-trmt112, 18s rrna methyltransferase, rrna methyltransferase bud23, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
WBSCR22-TRMT112
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SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:18S rRNA (guanine1575-N7)-methyltransferase
The enzyme, found in eukaryotes, is involved in pre-rRNA processing. The numbering corresponds to the enzyme from the yeast Saccharomyces cerevisiae [1].
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + guanine10 in tRNA
S-adenosyl-L-homocysteine + N2-methylguanine10 in tRNA
show the reaction diagram
m7G1639 methylation
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + guanine10 in tRNA
S-adenosyl-L-homocysteine + N2-methylguanine10 in tRNA
show the reaction diagram
m7G1639 methylation
-
-
?
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
S-adenosyl-L-methionine
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additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
TRMT112
a multifunctional methyltransferase subunit TRM112-like protein with methyltransferase activity, it participates both in methylation of protein and tRNA species. TRMT112 is required for WBSCR22 metabolic stability
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
WBS22; gene WBSCR22
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
WBSCR22-TRMT112 is the functional homologue of Saccharomyces cerevisiae Bud23-Trm112
malfunction
HeLa cells depleted of WBSCR22 show a mild reduction in 30S, indicative of reduced cleavage at site 2, and significant accumulation of 18S-E revealing inhibition of cleavage at site 3. Long and short truncated forms of 18S precursors are detected. On WBSCR22 depletion, the amount of mature 18S rRNA is markedly reduced and the 28S/18S rRNA ratio conse­quently increased. TRMT112 depletion leads to processing phenotypes largely similar to those observed upon WB­SCR22 depletion (moderate 30S reduction and accumulation of 18S-E). The processing defects do not depend on p53 and are essentially the same, with minor differences, in different cell types. Kinetics of the pre-rRNA processing defects in HeLa cells by in vivo metabolic labeling, phenotype, overview
metabolism
DIMT1L, WBSCR22, and TRMT112 are required for distinct pre-rRNA processing steps, and the pre-rRNA processing defects are conserved in different cell types and do not depend on p53
physiological function
the enzyme is required for distinct pre-rRNA processing reactions leading to synthesis of 18S rRNA. In human cells riboosome biogenesis requires the presence of the modification enzyme rather than its RNA-modifying catalytic activity. Methylation activity of WBSCR22-TRMT112 is not necessary for pre-rRNA processing
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
BUD23_HUMAN
281
0
31880
Swiss-Prot
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Zorbas, C.; Nicolas, E.; Wacheul, L.; Huvelle, E.; Heurgue-Hamard, V.; Lafontaine, D.L.
The human 18S rRNA base methyltransferases DIMT1L and WBSCR22-TRMT112 but not rRNA modification are required for ribosome biogenesis
Mol. Biol. Cell
26
2080-2095
2015
Homo sapiens (O43709), Homo sapiens
Manually annotated by BRENDA team