| pubmed-article:17389639 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:17389639 | lifeskim:mentions | umls-concept:C0035701 | lld:lifeskim |
| pubmed-article:17389639 | lifeskim:mentions | umls-concept:C0025831 | lld:lifeskim |
| pubmed-article:17389639 | lifeskim:mentions | umls-concept:C1521840 | lld:lifeskim |
| pubmed-article:17389639 | pubmed:issue | 7 | lld:pubmed |
| pubmed-article:17389639 | pubmed:dateCreated | 2007-5-2 | lld:pubmed |
| pubmed-article:17389639 | pubmed:abstractText | Five nearly universal methylated guanine-(N2) residues are present in bacterial rRNA in the ribosome. To date four out of five ribosomal RNA guanine-(N2)-methyltransferases are described. RsmC(YjjT) methylates G1207 of the 16S rRNA. RlmG(YgjO) and RlmL(YcbY) are responsible for the 23S rRNA m(2)G1835 and m(2)G2445 formation, correspondingly. RsmD(YhhF) is necessary for methylation of G966 residue of 16S rRNA. Structure of Escherichia coli RsmD(YhhF) methyltransferase and the structure of the Methanococcus jannaschii RsmC ortholog were determined. All ribosomal guanine-(N2)-methyltransferases have similar AdoMet-binding sites. In relation to the ribosomal substrate recognition, two enzymes that recognize assembled subunits are relatively small single domain proteins and two enzymes that recognize naked rRNA are larger proteins containing separate methyltransferase- and RNA-binding domains. The model for recognition of specific target nucleotide is proposed. The hypothetical role of the m(2)G residues in rRNA is discussed. | lld:pubmed |
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| pubmed-article:17389639 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:17389639 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:17389639 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:17389639 | pubmed:issn | 1362-4962 | lld:pubmed |
| pubmed-article:17389639 | pubmed:author | pubmed-author:DontsovaOlga... | lld:pubmed |
| pubmed-article:17389639 | pubmed:author | pubmed-author:BogdanovAlexe... | lld:pubmed |
| pubmed-article:17389639 | pubmed:author | pubmed-author:SergievPetr... | lld:pubmed |
| pubmed-article:17389639 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:17389639 | pubmed:volume | 35 | lld:pubmed |
| pubmed-article:17389639 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:17389639 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:17389639 | pubmed:pagination | 2295-301 | lld:pubmed |
| pubmed-article:17389639 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
| pubmed-article:17389639 | pubmed:meshHeading | pubmed-meshheading:17389639... | lld:pubmed |
| pubmed-article:17389639 | pubmed:meshHeading | pubmed-meshheading:17389639... | lld:pubmed |
| pubmed-article:17389639 | pubmed:meshHeading | pubmed-meshheading:17389639... | lld:pubmed |
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| pubmed-article:17389639 | pubmed:meshHeading | pubmed-meshheading:17389639... | lld:pubmed |
| pubmed-article:17389639 | pubmed:year | 2007 | lld:pubmed |
| pubmed-article:17389639 | pubmed:articleTitle | Ribosomal RNA guanine-(N2)-methyltransferases and their targets. | lld:pubmed |
| pubmed-article:17389639 | pubmed:affiliation | Department of Chemistry and A.N. Belozersky Institute of Physico-Chemical Biology, Moscow State University, Moscow, Russia. | lld:pubmed |
| pubmed-article:17389639 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:17389639 | pubmed:publicationType | Review | lld:pubmed |
| pubmed-article:17389639 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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