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| http://purl.uniprot.org/citations/17610498 | http://www.w3.org/2000/01/rdf-schema#comment | "Methylation is one of the most common protein modifications. Many different prokaryotic and eukaryotic proteins are methylated, including proteins involved in translation, including ribosomal proteins (RPs) and translation factors (TFs). Positions of the methylated residues in six Escherichia coli RPs and two Saccharomyces cerevisiae RPs have been determined. At least two RPs, L3 and L12, are methylated in both organisms. Both prokaryotic and eukaryotic elongation TFs (EF1A) are methylated at lysine residues, while both release factors are methylated at glutamine residues. The enzymes catalysing methylation reactions, protein methyltransferases (MTases), generally use S-adenosylmethionine as the methyl donor to add one to three methyl groups that, in case of arginine, can be asymetrically positioned. The biological significance of RP and TF methylation is poorly understood, and deletions of the MTase genes usually do not cause major phenotypes. Apparently methylation modulates intra- or intermolecular interactions of the target proteins or affects their affinity for RNA, and, thus, influences various cell processes, including transcriptional regulation, RNA processing, ribosome assembly, translation accuracy, protein nuclear trafficking and metabolism, and cellular signalling. Differential methylation of specific RPs and TFs in a number of organisms at different physiological states indicates that this modification may play a regulatory role."xsd:string |
| http://purl.uniprot.org/citations/17610498 | http://purl.org/dc/terms/identifier | "doi:10.1111/j.1365-2958.2007.05831.x"xsd:string |
| http://purl.uniprot.org/citations/17610498 | http://purl.uniprot.org/core/author | "Polevoda B."xsd:string |
| http://purl.uniprot.org/citations/17610498 | http://purl.uniprot.org/core/author | "Sherman F."xsd:string |
| http://purl.uniprot.org/citations/17610498 | http://purl.uniprot.org/core/date | "2007"xsd:gYear |
| http://purl.uniprot.org/citations/17610498 | http://purl.uniprot.org/core/name | "Mol Microbiol"xsd:string |
| http://purl.uniprot.org/citations/17610498 | http://purl.uniprot.org/core/pages | "590-606"xsd:string |
| http://purl.uniprot.org/citations/17610498 | http://purl.uniprot.org/core/title | "Methylation of proteins involved in translation."xsd:string |
| http://purl.uniprot.org/citations/17610498 | http://purl.uniprot.org/core/volume | "65"xsd:string |
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