Document Detail


How many EF-Tu molecules participate in aminoacyl-tRNA binding?
MedLine Citation:
PMID:  1742349     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
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].
Authors:
K Bensch; U Pieper; G Ott; N Schirmer; M Sprinzl; A Pingoud
Related Documents :
14645579 - Mechanism of action and antiviral activity of benzimidazole-based allosteric inhibitors...
16699189 - Novel crystal form of the cole1 rom protein.
1841379 - Structure-function relationship of hammerhead ribozymes as probed by 2'-modifications.
22618019 - Fluorescent probe for detection of bacteria: conformational trigger upon bacterial redu...
22400799 - Label-free catalytic and molecular beacon containing an abasic site for sensitive fluor...
12736309 - Zinc-dependent cleavage in the catalytic core of the hammerhead ribozyme: evidence for ...
730749 - Studies on the interaction of immobilized trypsin and specific ligands by quantitative ...
23484909 - Inhibition of dd-peptidases by a specific trifluoroketone: crystal structure of a compl...
21880019 - Dissecting structure-function-stability relationships of a thermostable gh5-cbm3 cellul...
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    
Affiliation:
Abteilung Biophysikalische Chemie, Zentrum Biochemie, Medizinische Hochschule Hannover, Germany.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:
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
Chemical
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

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


Previous Document:  Overproduction of the Thermus thermophilus elongation factor Tu in Escherichia coli.
Next Document:  Structure-function relationships of elongation factor Tu as studied by mutagenesis.