Document Detail


Evidence that a single GTP is used in the formation of 80 S initiation complexes.
MedLine Citation:
PMID:  438155     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Evidence is presented that the GTP initially bound in ternary complex (Met-tRNAf.GTP.eukaryotic initiation factor 2 (eIF-2)) is the same GTP that is hydrolyzed to allow joining of a 40 S preinitiation complex with 60 S subunits. This evidence was obtained by two quite dissimilar techniques. The first was a kinetic analysis of AUG-directed methionyl-puromycin synthesis using either eIF-2 of eIF-2A to direct the binding of Met-tRNAf to 40 S subunits. The second technique was the isolation of 40 S preinitiation complexes by Sepharose 6B chromatography and subsequent quantitation of GTP hydrolysis and methionyl-puromycin synthesis under conditions where 80 S complex formation is permitted.
Authors:
W C Merrick
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Publication Detail:
Type:  Journal Article; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  The Journal of biological chemistry     Volume:  254     ISSN:  0021-9258     ISO Abbreviation:  J. Biol. Chem.     Publication Date:  1979 May 
Date Detail:
Created Date:  1979-07-25     Completed Date:  1979-07-25     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  2985121R     Medline TA:  J Biol Chem     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  3708-11     Citation Subset:  IM    
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MeSH Terms
Descriptor/Qualifier:
Animals
Guanosine Triphosphate / metabolism*
Kinetics
Methionine
Peptide Chain Initiation, Translational*
Peptide Initiation Factors / metabolism*
RNA, Transfer / metabolism
Rabbits
Reticulocytes / metabolism
Chemical
Reg. No./Substance:
0/Peptide Initiation Factors; 63-68-3/Methionine; 86-01-1/Guanosine Triphosphate; 9014-25-9/RNA, Transfer

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


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