Document Detail

How many EF-Tu molecules participate in aminoacyl-tRNA binding?
MedLine Citation:
PMID:  1742349     Owner:  NLM     Status:  MEDLINE    
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].
K Bensch; U Pieper; G Ott; N Schirmer; M Sprinzl; A Pingoud
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Biochimie     Volume:  73     ISSN:  0300-9084     ISO Abbreviation:  Biochimie     Publication Date:    1991 Jul-Aug
Date Detail:
Created Date:  1992-01-16     Completed Date:  1992-01-16     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  1264604     Medline TA:  Biochimie     Country:  FRANCE    
Other Details:
Languages:  eng     Pagination:  1045-50     Citation Subset:  IM    
Abteilung Biophysikalische Chemie, Zentrum Biochemie, Medizinische Hochschule Hannover, Germany.
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MeSH Terms
Binding Sites
Chromatography, Gel
Escherichia coli / metabolism
Guanosine Triphosphate / metabolism
Peptide Elongation Factor Tu / metabolism*
RNA, Transfer, Amino Acyl / metabolism*
RNA, Transfer, Phe / metabolism
Spectrometry, Fluorescence
Reg. No./Substance:
0/RNA, Transfer, Amino Acyl; 0/RNA, Transfer, Phe; 86-01-1/Guanosine Triphosphate; EC 3.1.-/Ribonucleases; EC 3.6.1.-/Peptide Elongation Factor Tu

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