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rdf:type |
|
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lifeskim:mentions |
umls-concept:C0026882,
umls-concept:C0077361,
umls-concept:C0205252,
umls-concept:C0205314,
umls-concept:C0205369,
umls-concept:C0456387,
umls-concept:C0521009,
umls-concept:C0597603,
umls-concept:C0678594,
umls-concept:C0679622,
umls-concept:C1514562,
umls-concept:C1705535,
umls-concept:C1880389,
umls-concept:C1883204,
umls-concept:C1883221
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pubmed:issue |
4
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pubmed:dateCreated |
2010-2-15
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pubmed:abstractText |
The bacterial translation factor RF3 promotes translation termination by recycling the tRNA-mimicking release factors, RF1 and RF2, after mature polypeptide release. RF3 also enhances the premature peptidyl-tRNA drop-off reaction in the presence of RRF and EF-G. Despite the recently resolved X-ray crystal structure of RF3, the molecular details of the bimodal functionality of RF3 remain obscure. In this report, we demonstrate a novel class of RF3 mutations specifically defective in the tRNA drop-off reaction. These mutations suggest differential molecular pathways closely related to the guanine nucleotide modes of RF3.
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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 |
Feb
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pubmed:issn |
1873-3468
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pubmed:author |
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pubmed:copyrightInfo |
Copyright 2009 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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pubmed:issnType |
Electronic
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pubmed:day |
19
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pubmed:volume |
584
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
790-4
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pubmed:meshHeading |
pubmed-meshheading:20043913-Base Sequence,
pubmed-meshheading:20043913-Binding Sites,
pubmed-meshheading:20043913-Escherichia coli,
pubmed-meshheading:20043913-Escherichia coli Proteins,
pubmed-meshheading:20043913-Models, Molecular,
pubmed-meshheading:20043913-Mutation,
pubmed-meshheading:20043913-Peptide Termination Factors,
pubmed-meshheading:20043913-Protein Conformation,
pubmed-meshheading:20043913-Protein Structure, Tertiary,
pubmed-meshheading:20043913-RNA, Transfer, Amino Acyl,
pubmed-meshheading:20043913-Structure-Activity Relationship
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pubmed:year |
2010
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pubmed:articleTitle |
A novel class of bacterial translation factor RF3 mutations suggests specific structural domains for premature peptidyl-tRNA drop-off.
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pubmed:affiliation |
Department of Basic Medical Sciences, Institute of Medical Science, University of Tokyo (IMSUT), Tokyo, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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