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Information on EC 2.1.1.310 - 25S rRNA (cytosine2870-C5)-methyltransferase and Organism(s) Saccharomyces cerevisiae and UniProt Accession P40991

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IUBMB Comments
The enzyme, found in eukaryotes, is specific for cytosine2870 of the 25S ribosomal RNA. The numbering corresponds to the enzyme from the yeast Saccharomyces cerevisiae .
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This record set is specific for:
Saccharomyces cerevisiae
UNIPROT: P40991
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The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Synonyms
protein p120, proliferation-associated nucleolar antigen, m5c-methyltransferase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
m5C-methyltransferase
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RNA:m5C-MTase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + cytosine2870 in 25S rRNA = S-adenosyl-L-homocysteine + 5-methylcytosine2870 in 25S rRNA
show the reaction diagram
one of the catalytic cysteines in the m5C-MTase active site is required for initial attack to target cytosine, while the second serves for recycling function during the product release
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SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:25S rRNA (cytosine2870-C5)-methyltransferase
The enzyme, found in eukaryotes, is specific for cytosine2870 of the 25S ribosomal RNA. 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 + cytosine2870 in 25S rRNA
S-adenosyl-L-homocysteine + 5-methylcytosine2870 in 25S rRNA
show the reaction diagram
S-adenosyl-L-methionine + cytosine2870 in 25S rRNA
S-adenosyl-L-homocysteine + 5-methylcytosine2870 in 25S rRNA
show the reaction diagram
additional information
?
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no evidence of m5C residues in yeast 18S rRNA
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?
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 + cytosine2870 in 25S rRNA
S-adenosyl-L-homocysteine + 5-methylcytosine2870 in 25S rRNA
show the reaction diagram
the enzyme is responsible for the methylation at cytosine2870 of the 25S ribosomal RNA
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?
S-adenosyl-L-methionine + cytosine2870 in 25S rRNA
S-adenosyl-L-homocysteine + 5-methylcytosine2870 in 25S rRNA
show the reaction diagram
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yeast proteins Nop2p and Rcm1p catalyze the formation of m5C in domains V and IV, respectively
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?
additional information
?
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no evidence of m5C residues in yeast 18S rRNA
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?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
S-adenosyl-L-methionine
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
the N-terminal domain of the enzyme is important for its nucleolar localization
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
the loss of m5C2870 affects ribosome synthesis and processing
evolution
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the enzyme is a member of a protein family called Nop2/NSUN/NOL1. Nop2 belongs to the large family of pre-ribosomal proteins
malfunction
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strains expressing Nop2DELTA(1-220) are viable, but exhibit a significant growth defect
metabolism
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Nop2 and Rcm1 catalyze m5C formation in large subunit yeast rRNA, Nop2 forms 25S rRNA m5C2870, while Rcm1 forms 25S rRNA m5C2278
physiological function
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nucleolar protein Nop2 is required for production of 25S rRNA and, consequently, during the biogenesis of 60S ribosomal subunits. Nop2 forms 25S rRNA m5C2870. the enzyme possesses two related functions in pre-rRNA processing: as an essential factor for cleavages and m5C:RNA:modification. The presence of Nop2, rather than the m5C modification in rRNA itself, is required for pre-rRNA processing
additional information
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importance of different sequence and structural domains of Nop2 and p120 for yeast growth and m5C-MTase activity, importance of Nop2 N-terminal domain for correct protein localization and its cellular function, overview
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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enzyme protein domain structure, overview
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C478A
the polysome profile from the mutant reveals defect in 60S biogenesis and significant reduction in polysome fractions compared with isogenic wild type
additional information
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functional complementation of Nop2-deficient yeasts by human protein p120, the N-terminal domain of Nop2 is essential for efficient complementation by p120 in yeast. Generation of GFP-tagged chimeric protein formed by Nop2 and human p120 fragments. The HYB protein, which is composed of N-terminal Nop2 and C-terminal p120 domains, efficiently localizes within the nucleolus, demonstrating that all necessary cell sorting signals are indeed located in the Nop2 N-terminal domain. The yeast strain expressing N-terminal domain-truncated Nop2 is not viable, indicating that localization of Nop2 is important for its function. A double mutant of Nop2 protein with two mutated cysteines that are expected to be involved in catalysis, namely Cys424 and Cys478, shows no phenotype
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged full-length Nop2 and Nop2(1-220) N-terminal domain from Escherichia coli strain BL21(DE3) CodonPlus by polyethyleneimine precipitation, anion exchange and nickel affinity chromatography, followed by dialysis
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cloning from genomic DNA, recombinant expression of His-tagged full-length Nop2 and Nop2(1-220) N-terminal domain in Escherichia coli strain BL21(DE3) CodonPlus
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Sharma, S.; Yang, J.; Watzinger, P.; Koetter, P.; Entian, K.D.
Yeast Nop2 and Rcm1 methylate C2870 and C2278 of the 25S rRNA, respectively
Nucleic Acids Res.
41
9062-9076
2013
Saccharomyces cerevisiae (P40991), Saccharomyces cerevisiae ATCC 204508 (P40991)
Manually annotated by BRENDA team
Bourgeois, G.; Ney, M.; Gaspar, I.; Aigueperse, C.; Schaefer, M.; Kellner, S.; Helm, M.; Motorin, Y.
Eukaryotic rRNA modification by yeast 5-methylcytosine-methyltransferases and human proliferation-associated antigen p120
PLoS ONE
10
e0133321
2015
Homo sapiens, Saccharomyces cerevisiae, Saccharomyces cerevisiae BY4742
Manually annotated by BRENDA team