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PMID: 1742349 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

How many EF-Tu molecules participate in aminoacyl-tRNA binding?

Biochimie ·Vol. 73 ·No. 7-8 ·1991-00-00 ·Pages 1045-50

Bensch K, Pieper U, Ott G, Schirmer N, Sprinzl M, Pingoud A

Abstract

The stoichiometry of the EF-Tu-GTP-aminoacyl-tRNA complex has been re-determined by a variety of methods, viz gel filtrations, fluorescence titrations, as well as hydrolysis and RNase protection experiments. The results of these experiments clearly demonstrate that one aminoacyl-tRNA interacts with only one EF-Tu-GTP molecule, in agreement with the established view and in contrast to the recently published results by Ehrenberg et al [6].

MeSH Terms
Binding Sites Chromatography, Gel Escherichia coli/metabolism Guanosine Triphosphate/metabolism Hydrolysis Peptide Elongation Factor Tu/metabolism RNA, Transfer, Amino Acyl/metabolism RNA, Transfer, Phe/metabolism Ribonucleases Spectrometry, Fluorescence
Chemicals
RNA, Transfer, Amino Acyl RNA, Transfer, Phe Guanosine Triphosphate Ribonucleases Peptide Elongation Factor Tu
Authors & Affiliations
6 authors, click to expand affiliations / ORCID
Bensch K
Abteilung Biophysikalische Chemie, Zentrum Biochemie, Medizinische Hochschule Hannover, Germany.
Pieper U
Ott G
Schirmer N
Sprinzl M
Pingoud A
Article Info
Journal
Biochimie
Abbr.
Biochimie
ISSN
0300-9084
Published
1991-00-00
Pages
1045-50
Language
English
Region
France
NLM ID
1264604
Subset
IM
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