Source:http://linkedlifedata.com/resource/pubmed/id/19172743
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
9
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pubmed:dateCreated |
2009-1-27
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pubmed:databankReference | |
pubmed:abstractText |
EF4 (LepA) is an almost universally conserved translational GTPase in eubacteria. It seems to be essential under environmental stress conditions and has previously been shown to back-translocate the tRNAs on the ribosome, thereby reverting the canonical translocation reaction. In the current work, EF4 was directly visualized in the process of back-translocating tRNAs by single-particle cryo-EM. Using flexible fitting methods, we built a model of ribosome-bound EF4 based on the cryo-EM map and a recently published unbound EF4 X-ray structure. The cryo-EM map establishes EF4 as a noncanonical elongation factor that interacts not only with the elongating ribosome, but also with the back-translocated tRNA in the A-site region, which is present in a previously unseen, intermediate state and deviates markedly from the position of a canonical A-tRNA. Our results, therefore, provide insight into the underlying structural principles governing back-translocation.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Escherichia coli Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Guanosine Triphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/LepA protein, E coli,
http://linkedlifedata.com/resource/pubmed/chemical/Macromolecular Substances,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Bacterial,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Transfer,
http://linkedlifedata.com/resource/pubmed/chemical/Transcriptional Elongation Factors
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
1545-9993
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
15
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
910-5
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pubmed:meshHeading |
pubmed-meshheading:19172743-Biological Transport, Active,
pubmed-meshheading:19172743-Escherichia coli,
pubmed-meshheading:19172743-Escherichia coli Proteins,
pubmed-meshheading:19172743-Guanosine Triphosphate,
pubmed-meshheading:19172743-Hydrolysis,
pubmed-meshheading:19172743-Macromolecular Substances,
pubmed-meshheading:19172743-Models, Molecular,
pubmed-meshheading:19172743-RNA, Bacterial,
pubmed-meshheading:19172743-RNA, Transfer,
pubmed-meshheading:19172743-Ribosomes,
pubmed-meshheading:19172743-Transcriptional Elongation Factors
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pubmed:year |
2008
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pubmed:articleTitle |
A new tRNA intermediate revealed on the ribosome during EF4-mediated back-translocation.
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pubmed:affiliation |
Institut für Medizinische Physik und Biophysik, Charite-Universitätsmedizin Berlin, Ziegelstrasse 5-9, 10117-Berlin, Germany.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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