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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The enzyme appears in viruses and cellular organisms
S-adenosyl-L-methionine + cytosine2870 in 25S rRNA = S-adenosyl-L-homocysteine + 5-methylcytosine2870 in 25S rRNA
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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
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
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].
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
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
The prognostic significance of proliferation-associated nucleolar protein p120 expression in prostate adenocarcinoma: a comparison with cyclins A and B1, Ki-67, proliferating cell nuclear antigen, and p34cdc2.
Analysis of a 17.4 kb DNA segment of yeast chromosome II encompassing the ribosomal protein L19 as well as proteins with homologies to components of the hnRNP and snRNP complexes and to the human proliferation-associated p120 antigen.
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
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
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
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
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
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
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
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
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
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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, 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
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
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