Document Detail

Incorporation of glutamic acid into protein by a soluble system.
MedLine Citation:
PMID:  6134720     Owner:  NLM     Status:  MEDLINE    
A heat-labile, non-dialyzable factor(s) in soluble fractions from Escherichia coli strains and Bacillus subtilis was found to incorporate the radioactivity of [14C]glutamic acid into 95 degrees C CCl3COOH-insoluble fraction. Incorporation catalyzed by a partially purified factor from E. coli B required ATP, Mg2+, tRNA, casein, carbonate, and 2-mercaptoethanol. A mixture of nineteen amino acids other than glutamic acid had no effect on the incorporation. Heparin, spermine and monovalent cations were inhibitory. Incorporation proceeded via glutamyl-tRNA. The incorporation from [14C]glutamyl-tRNA required Mg2+, casein, carbonate, and 2-mercaptoethanol, and there was no incorporation from [14C]aspartyl-tRNA. The reaction product was identified as protein. The incorporated moiety was the glutamyl moiety of glutamic acid and it retained a free alpha-amino group in the product protein. The incorporating factor of E. coli B was demonstrated to be glutamyl-tRNA synthetase.
S Hashizume; T Honjoh; M Shoji
Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Journal of biochemistry     Volume:  93     ISSN:  0021-924X     ISO Abbreviation:  J. Biochem.     Publication Date:  1983 Apr 
Date Detail:
Created Date:  1983-08-11     Completed Date:  1983-08-11     Revised Date:  2007-12-19    
Medline Journal Info:
Nlm Unique ID:  0376600     Medline TA:  J Biochem     Country:  JAPAN    
Other Details:
Languages:  eng     Pagination:  1109-18     Citation Subset:  IM    
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MeSH Terms
Bacillus subtilis / metabolism*
Bacterial Proteins / biosynthesis*
Escherichia coli / metabolism*
Glutamate-tRNA Ligase / metabolism
Glutamates / metabolism*
Glutamic Acid
Time Factors
Reg. No./Substance:
0/Bacterial Proteins; 0/Glutamates; 56-86-0/Glutamic Acid; EC Ligase

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

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