| pubmed-article:20224578 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:20224578 | lifeskim:mentions | umls-concept:C1552144 | lld:lifeskim |
| pubmed-article:20224578 | lifeskim:mentions | umls-concept:C0083982 | lld:lifeskim |
| pubmed-article:20224578 | lifeskim:mentions | umls-concept:C1704686 | lld:lifeskim |
| pubmed-article:20224578 | lifeskim:mentions | umls-concept:C0439855 | lld:lifeskim |
| pubmed-article:20224578 | lifeskim:mentions | umls-concept:C0887977 | lld:lifeskim |
| pubmed-article:20224578 | pubmed:issue | 4 | lld:pubmed |
| pubmed-article:20224578 | pubmed:dateCreated | 2010-3-30 | lld:pubmed |
| pubmed-article:20224578 | pubmed:abstractText | Bacterial translation initiation factor 2 (IF2) is a GTPase that promotes the binding of the initiator fMet-tRNA(fMet) to the 30S ribosomal subunit. It is often assumed that IF2 delivers fMet-tRNA(fMet) to the ribosome in a ternary complex, IF2.GTP.fMet-tRNA(fMet). By using rapid kinetic techniques, we show here that binding of IF2.GTP to the 30S ribosomal subunit precedes and is independent of fMet-tRNA(fMet) binding. The ternary complex formed in solution by IF2.GTP and fMet-tRNA is unstable and dissociates before IF2.GTP and, subsequently, fMet-tRNA(fMet) bind to the 30S subunit. Ribosome-bound IF2 might accelerate the recruitment of fMet-tRNA(fMet) to the 30S initiation complex by providing anchoring interactions or inducing a favourable ribosome conformation. The mechanism of action of IF2 seems to be different from that of tRNA carriers such as EF-Tu, SelB and eukaryotic initiation factor 2 (eIF2), instead resembling that of eIF5B, the eukaryotic subunit association factor. | lld:pubmed |
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| pubmed-article:20224578 | pubmed:language | eng | lld:pubmed |
| pubmed-article:20224578 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20224578 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:20224578 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20224578 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20224578 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20224578 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:20224578 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:20224578 | pubmed:issn | 1469-3178 | lld:pubmed |
| pubmed-article:20224578 | pubmed:author | pubmed-author:RodninaMarina... | lld:pubmed |
| pubmed-article:20224578 | pubmed:author | pubmed-author:GualerziClaud... | lld:pubmed |
| pubmed-article:20224578 | pubmed:author | pubmed-author:WintermeyerWo... | lld:pubmed |
| pubmed-article:20224578 | pubmed:author | pubmed-author:KonevegaAndre... | lld:pubmed |
| pubmed-article:20224578 | pubmed:author | pubmed-author:MilonPohlP | lld:pubmed |
| pubmed-article:20224578 | pubmed:author | pubmed-author:CarottiMarcel... | lld:pubmed |
| pubmed-article:20224578 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:20224578 | pubmed:volume | 11 | lld:pubmed |
| pubmed-article:20224578 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:20224578 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:20224578 | pubmed:pagination | 312-6 | lld:pubmed |
| pubmed-article:20224578 | pubmed:dateRevised | 2011-7-27 | lld:pubmed |
| pubmed-article:20224578 | pubmed:meshHeading | pubmed-meshheading:20224578... | lld:pubmed |
| pubmed-article:20224578 | pubmed:meshHeading | pubmed-meshheading:20224578... | lld:pubmed |
| pubmed-article:20224578 | pubmed:meshHeading | pubmed-meshheading:20224578... | lld:pubmed |
| pubmed-article:20224578 | pubmed:meshHeading | pubmed-meshheading:20224578... | lld:pubmed |
| pubmed-article:20224578 | pubmed:meshHeading | pubmed-meshheading:20224578... | lld:pubmed |
| pubmed-article:20224578 | pubmed:meshHeading | pubmed-meshheading:20224578... | lld:pubmed |
| pubmed-article:20224578 | pubmed:meshHeading | pubmed-meshheading:20224578... | lld:pubmed |
| pubmed-article:20224578 | pubmed:year | 2010 | lld:pubmed |
| pubmed-article:20224578 | pubmed:articleTitle | The ribosome-bound initiation factor 2 recruits initiator tRNA to the 30S initiation complex. | lld:pubmed |
| pubmed-article:20224578 | pubmed:affiliation | Department of Physical Biochemistry, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, Göttingen 37077, Germany. | lld:pubmed |
| pubmed-article:20224578 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:20224578 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:20224578 | lld:pubmed |
