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Literature summary for 2.1.1.310 extracted from

  • 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 (2015), PLoS ONE, 10, e0133321.
    View publication on PubMedView publication on EuropePMC

Application

Application Comment Organism
diagnostics whereas protein p120 is almost undetectable in normal tissues, it is overexpressed in virtually all types of cancer cells and is therefore considered to be a predictive cancer marker Homo sapiens

Cloned(Commentary)

Cloned (Comment) Organism
cloning from genomic DNA, expression in a Saccharomyces cerevisiae Nop2 enzyme mutant and partial complementation. Full-length human p120 when expressed in Saccharomyces cerevisiae strongly accumulates in the nucleolus Homo sapiens
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 Saccharomyces cerevisiae

Protein Variants

Protein Variants Comment Organism
additional information 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 Saccharomyces cerevisiae
additional information generation of GFP-tagged chimeric protein formed by yeast Nop2 and 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 Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
nucleolus the N-terminal domain of the enzyme is important for its nucleolar localization Saccharomyces cerevisiae 5730
-
nucleus
-
Saccharomyces cerevisiae 5634
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Saccharomyces cerevisiae no evidence of m5C residues in yeast 18S rRNA ?
-
?
additional information Homo sapiens protein p120 displays an RNA:m5C-MTase activity, which restores m5C formation at position 2870 in domain V of 25S rRNA in a nop2DELTA yeast strain, functional complementation of Nop2-deficient yeasts by human protein p120 ?
-
?
additional information Saccharomyces cerevisiae BY4742 no evidence of m5C residues in yeast 18S rRNA ?
-
?
S-adenosyl-L-methionine + cytosine2870 in 25S rRNA Homo sapiens
-
S-adenosyl-L-homocysteine + 5-methylcytosine2870 in 25S rRNA
-
?
S-adenosyl-L-methionine + cytosine2870 in 25S rRNA Saccharomyces cerevisiae yeast proteins Nop2p and Rcm1p catalyze the formation of m5C in domains V and IV, respectively S-adenosyl-L-homocysteine + 5-methylcytosine2870 in 25S rRNA
-
?
S-adenosyl-L-methionine + cytosine2870 in 25S rRNA Saccharomyces cerevisiae BY4742 yeast proteins Nop2p and Rcm1p catalyze the formation of m5C in domains V and IV, respectively S-adenosyl-L-homocysteine + 5-methylcytosine2870 in 25S rRNA
-
?

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-
Saccharomyces cerevisiae
-
-
-
Saccharomyces cerevisiae BY4742
-
-
-

Purification (Commentary)

Purification (Comment) Organism
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 Saccharomyces cerevisiae

Reaction

Reaction Comment Organism Reaction ID
S-adenosyl-L-methionine + cytosine2870 in 25S rRNA = S-adenosyl-L-homocysteine + 5-methylcytosine2870 in 25S rRNA 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 Saccharomyces cerevisiae

Source Tissue

Source Tissue Comment Organism Textmining
additional information whereas protein p120 is almost undetectable in normal tissues, it is overexpressed in virtually all types of cancer cells. The enzyme concentration varies during the cell cycle, reaching its maximum value in the G2 phase Homo sapiens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information no evidence of m5C residues in yeast 18S rRNA Saccharomyces cerevisiae ?
-
?
additional information protein p120 displays an RNA:m5C-MTase activity, which restores m5C formation at position 2870 in domain V of 25S rRNA in a nop2DELTA yeast strain, functional complementation of Nop2-deficient yeasts by human protein p120 Homo sapiens ?
-
?
additional information no evidence of m5C residues in yeast 18S rRNA Saccharomyces cerevisiae BY4742 ?
-
?
S-adenosyl-L-methionine + cytosine2870 in 25S rRNA
-
Homo sapiens S-adenosyl-L-homocysteine + 5-methylcytosine2870 in 25S rRNA
-
?
S-adenosyl-L-methionine + cytosine2870 in 25S rRNA
-
Saccharomyces cerevisiae S-adenosyl-L-homocysteine + 5-methylcytosine2870 in 25S rRNA
-
?
S-adenosyl-L-methionine + cytosine2870 in 25S rRNA yeast proteins Nop2p and Rcm1p catalyze the formation of m5C in domains V and IV, respectively Saccharomyces cerevisiae S-adenosyl-L-homocysteine + 5-methylcytosine2870 in 25S rRNA
-
?
S-adenosyl-L-methionine + cytosine2870 in 25S rRNA
-
Saccharomyces cerevisiae BY4742 S-adenosyl-L-homocysteine + 5-methylcytosine2870 in 25S rRNA
-
?
S-adenosyl-L-methionine + cytosine2870 in 25S rRNA yeast proteins Nop2p and Rcm1p catalyze the formation of m5C in domains V and IV, respectively Saccharomyces cerevisiae BY4742 S-adenosyl-L-homocysteine + 5-methylcytosine2870 in 25S rRNA
-
?

Subunits

Subunits Comment Organism
More enzyme protein domain structure, overview Homo sapiens
More enzyme protein domain structure, overview Saccharomyces cerevisiae

Synonyms

Synonyms Comment Organism
m5C-methyltransferase
-
Homo sapiens
m5C-methyltransferase
-
Saccharomyces cerevisiae
NOP2
-
Saccharomyces cerevisiae
NSUN1/Nol1
-
Homo sapiens
p120
-
Homo sapiens
proliferation-associated nucleolar antigen
-
Homo sapiens
protein p120
-
Homo sapiens
RNA:m5C-MTase
-
Homo sapiens
RNA:m5C-MTase
-
Saccharomyces cerevisiae

Cofactor

Cofactor Comment Organism Structure
S-adenosyl-L-methionine
-
Homo sapiens
S-adenosyl-L-methionine
-
Saccharomyces cerevisiae

General Information

General Information Comment Organism
evolution the enzyme is a member of a protein family called Nop2/NSUN/NOL1. Nop2 belongs to the large family of pre-ribosomal proteins Saccharomyces cerevisiae
evolution the enzyme is a member of a protein family called Nop2/NSUN/NOL1. The human genome contains at least 9 genes encoding putative RNA:m5C-MTases which share sequence similarities with yeast Nop2/Trm4/Rcm1 Homo sapiens
malfunction strains expressing Nop2DELTA(1-220) are viable, but exhibit a significant growth defect Saccharomyces cerevisiae
metabolism Nop2 and Rcm1 catalyze m5C formation in large subunit yeast rRNA, Nop2 forms 25S rRNA m5C2870, while Rcm1 forms 25S rRNA m5C2278 Saccharomyces cerevisiae
additional information 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 Saccharomyces cerevisiae
physiological function 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 Saccharomyces cerevisiae
physiological function p120 forms 28S rRNA m5C4447. It is required for the G1/S transition Homo sapiens