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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2
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pubmed:dateCreated |
2000-9-28
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pubmed:abstractText |
Elongation factor G (EF-G) from Escherichia coli is a large, five-domain GTPase that promotes tRNA translocation on the ribosome. Full activity requires GTP hydrolysis, suggesting that a conformational change of the factor is important for function. To restrict the intramolecular mobility, two cysteine residues were engineered into domains 1 and 5 of EF-G that spontaneously formed a disulfide cross-link. Cross-linked EF-G retained GTPase activity on the ribosome, whereas it was inactive in translocation as well as in turnover. Both activities were restored when the cross-link was reversed by reduction. These results strongly argue against a GTPase switch-type model of EF-G function and demonstrate that conformational mobility is an absolute requirement for EF-G function on the ribosome.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
1097-2765
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
6
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
501-5
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:10983996-Amino Acid Substitution,
pubmed-meshheading:10983996-Cross-Linking Reagents,
pubmed-meshheading:10983996-Cysteine,
pubmed-meshheading:10983996-Escherichia coli,
pubmed-meshheading:10983996-GTP Phosphohydrolases,
pubmed-meshheading:10983996-Guanosine Diphosphate,
pubmed-meshheading:10983996-Kinetics,
pubmed-meshheading:10983996-Models, Molecular,
pubmed-meshheading:10983996-Mutagenesis, Site-Directed,
pubmed-meshheading:10983996-Peptide Elongation Factor G,
pubmed-meshheading:10983996-Protein Conformation,
pubmed-meshheading:10983996-RNA, Transfer,
pubmed-meshheading:10983996-Recombinant Proteins,
pubmed-meshheading:10983996-Ribosomes,
pubmed-meshheading:10983996-Thermus thermophilus
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pubmed:year |
2000
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pubmed:articleTitle |
Conformationally restricted elongation factor G retains GTPase activity but is inactive in translocation on the ribosome.
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pubmed:affiliation |
Institute of Molecular Biology, University of Witten/Herdecke, Witten, Germany.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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