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tRNA-ribosome interactions
Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Molecular Biology.
Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Molecular Biology.
Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Molecular Biology.
Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Molecular Biology.
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1995 (English)In: Biochemistry and Cell Biology, ISSN 0829-8211, E-ISSN 1208-6002, Vol. 73, no 11-12, 1049-1054 p.Article, review/survey (Refereed) Published
Abstract [en]

Direct measurements of the rates of dissociation of dipeptidyl-tRNA from the ribosome show that hyperaccurate SmP and SmD ribosomes have unstable A-site binding of peptidyl-tRNA, while P-site binding is extremely stable in relation to the wild type. Error-prone Ram ribosomes, on the other hand, have stable A-site and unstable P-site binding of peptidyl-tRNA. At least for these mutant ribosomes, we conclude that stabilization of peptidyl-tRNA in one site destabilizes binding in the other. Elongation factor Tu (EF-Tu) undergoes a dramatic structural transition from its GDP-bound form to its active GTP-bound form, in which it binds aa-tRNA (aminoacyl-tRNA) in ternary complex. The effects of substitution mutations at three sites in domain I of EF-Tu, Gln124, Leu120, and Tyr160, all of which point into the domain I-domain III interface in both the GTP and GDP conformations of EF-Tu, were examined. Mutations at each position cause large reductions in aa-tRNA binding. An attractive possibility is that the mutations alter the domain I-domain III interface such that the switching of EF-Tu between different conformations is altered, decreasing the probability of aa-tRNA binding. We have previously found that two GTPs are hydrolyzed per peptide bond on EF-Tu, the implication being that two molecules of EF-Tu may interact on the ribosome to catalyze the binding of a single aa-tRNA to the A-site. More recently we found that ribosomes programmed with mRNA constructs other than poly(U), including the sequence AUGUUUACG, invariably use two GTPs per peptide bond in EF-Tu function. Other experiments measuring the protection of aa-tRNA from deacylation or from RNAse A attack show that protection requires two molecules of EF-Tu, suggesting an extended ternary complex. To remove remaining ambiguities in the interpretion of these experiments, we are making direct molecular weight determinations with neutron scattering and sedimentation-diffusion techniques.

Place, publisher, year, edition, pages
1995. Vol. 73, no 11-12, 1049-1054 p.
Keyword [en]
bacterial protein, bacterial RNA, elongation factor Tu, transfer RNA, genetic selection, metabolism, molecular genetics, nucleotide sequence, reproducibility, review, ribosome
National Category
Natural Sciences
Identifiers
URN: urn:nbn:se:uu:diva-80254OAI: oai:DiVA.org:uu-80254DiVA: diva2:108168
Available from: 2008-10-17 Created: 2008-10-17 Last updated: 2017-12-14Bibliographically approved

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Hughes, Diarmaid

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