| pubmed-article:7782317 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:7782317 | lifeskim:mentions | umls-concept:C0031715 | lld:lifeskim |
| pubmed-article:7782317 | lifeskim:mentions | umls-concept:C0030933 | lld:lifeskim |
| pubmed-article:7782317 | lifeskim:mentions | umls-concept:C0439855 | lld:lifeskim |
| pubmed-article:7782317 | lifeskim:mentions | umls-concept:C1522492 | lld:lifeskim |
| pubmed-article:7782317 | lifeskim:mentions | umls-concept:C1292733 | lld:lifeskim |
| pubmed-article:7782317 | pubmed:issue | 24 | lld:pubmed |
| pubmed-article:7782317 | pubmed:dateCreated | 1995-7-17 | lld:pubmed |
| pubmed-article:7782317 | pubmed:abstractText | The elongation factor Tu (EF-Tu) is a member of the GTP/GDP-binding proteins and interacts with various partners during the elongation cycle of protein biosynthesis thereby mediating the correct binding of amino-acylated transfer RNA (aa-tRNA) to the acceptor site (A-site) of the ribosome. After GTP hydrolysis EF-Tu is released in its GDP-bound state. In vivo, EF-Tu is post-translationally modified by phosphorylation. Here we report that the phosphorylation of EF-Tu by a ribosome associated kinase activity is drastically enhanced by EF-Ts. The antibiotic kirromycin, known to block EF-Tu function, inhibits the modification. This effect is specific, since kirromycin-resistant mutants do become phosphorylated in the presence of the antibiotic. On the other hand, phosphorylated wild-type EF-Tu does not bind kirromycin. Most interestingly, the phosphorylation of EF-Tu abolishes its ability to bind aa-tRNA. In the GTP conformation the site of modification is located at the interface between domains 1 and 3 and is involved in a strong interdomain hydrogen bond. Introduction of a charged phosphate group at this position will change the interaction between the domains, leading to an opening of the molecule reminiscent of the GDP conformation. A model for the function of EF-Tu phosphorylation in protein biosynthesis is presented. | lld:pubmed |
| pubmed-article:7782317 | pubmed:language | eng | lld:pubmed |
| pubmed-article:7782317 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7782317 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:7782317 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7782317 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7782317 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7782317 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7782317 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7782317 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7782317 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7782317 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:7782317 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:7782317 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:7782317 | pubmed:author | pubmed-author:AlexanderCC | lld:pubmed |
| pubmed-article:7782317 | pubmed:author | pubmed-author:KraalBB | lld:pubmed |
| pubmed-article:7782317 | pubmed:author | pubmed-author:ErdmannV AVA | lld:pubmed |
| pubmed-article:7782317 | pubmed:author | pubmed-author:LippmannCC | lld:pubmed |
| pubmed-article:7782317 | pubmed:author | pubmed-author:LindschauCC | lld:pubmed |
| pubmed-article:7782317 | pubmed:author | pubmed-author:HilgenfeldRR | lld:pubmed |
| pubmed-article:7782317 | pubmed:author | pubmed-author:BilginNN | lld:pubmed |
| pubmed-article:7782317 | pubmed:author | pubmed-author:MestersJ RJR | lld:pubmed |
| pubmed-article:7782317 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:7782317 | pubmed:day | 16 | lld:pubmed |
| pubmed-article:7782317 | pubmed:volume | 270 | lld:pubmed |
| pubmed-article:7782317 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:7782317 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:7782317 | pubmed:pagination | 14541-7 | lld:pubmed |
| pubmed-article:7782317 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:7782317 | pubmed:meshHeading | pubmed-meshheading:7782317-... | lld:pubmed |
| pubmed-article:7782317 | pubmed:meshHeading | pubmed-meshheading:7782317-... | lld:pubmed |
| pubmed-article:7782317 | pubmed:meshHeading | pubmed-meshheading:7782317-... | lld:pubmed |
| pubmed-article:7782317 | pubmed:meshHeading | pubmed-meshheading:7782317-... | lld:pubmed |
| pubmed-article:7782317 | pubmed:meshHeading | pubmed-meshheading:7782317-... | lld:pubmed |
| pubmed-article:7782317 | pubmed:meshHeading | pubmed-meshheading:7782317-... | lld:pubmed |
| pubmed-article:7782317 | pubmed:meshHeading | pubmed-meshheading:7782317-... | lld:pubmed |
| pubmed-article:7782317 | pubmed:meshHeading | pubmed-meshheading:7782317-... | lld:pubmed |
| pubmed-article:7782317 | pubmed:meshHeading | pubmed-meshheading:7782317-... | lld:pubmed |
| pubmed-article:7782317 | pubmed:meshHeading | pubmed-meshheading:7782317-... | lld:pubmed |
| pubmed-article:7782317 | pubmed:meshHeading | pubmed-meshheading:7782317-... | lld:pubmed |
| pubmed-article:7782317 | pubmed:year | 1995 | lld:pubmed |
| pubmed-article:7782317 | pubmed:articleTitle | Phosphorylation of elongation factor Tu prevents ternary complex formation. | lld:pubmed |
| pubmed-article:7782317 | pubmed:affiliation | Institut für Biochemie, Freie Universität Berlin, Dahlem, Germany. | lld:pubmed |
| pubmed-article:7782317 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:7782317 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| entrez-gene:944866 | entrezgene:pubmed | pubmed-article:7782317 | lld:entrezgene |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:7782317 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:7782317 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:7782317 | lld:pubmed |
