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Mutations in ribosomal proteins L7/L12 perturb EF-G and EF-Tu functons
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. (Kurland)
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.
1988 (English)In: Biochimie, ISSN 0300-9084, E-ISSN 1638-6183, Vol. 70, no 5, 611-618 p.Article in journal (Refereed) Published
Abstract [en]

In vitro cycling rates of E. coli ribosomes and of elongation factors EF-Tu and EF-G have been obtained and these are compatible with translation rates in vivo. We show that the rate of translocation is faster than 50 s-1 and therefore that the EF-G function is not a rate limiting step in protein synthesis. The in vivo phenotype of some L7/L12 mutants could be accounted for by perturbed EF-Tu as well as EF-G functions. The S12 mutants that we studied were, in contrast, only perturbed in their EF-Tu function, while their EF-G interaction was not impaired in relation to wild type ribosomes.

Place, publisher, year, edition, pages
1988. Vol. 70, no 5, 611-618 p.
Keyword [en]
ribosomal mutants, in vitro translation
National Category
Natural Sciences
Identifiers
URN: urn:nbn:se:uu:diva-147814DOI: 10.1016/0300-9084(88)90244-1PubMedID: 3139080OAI: oai:DiVA.org:uu-147814DiVA: diva2:400887
Available from: 2011-02-28 Created: 2011-02-28 Last updated: 2017-12-11Bibliographically approved

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