Incorporation of glutamic acid into protein by a soluble system.

Abstract:

: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.

journal_name

J Biochem

journal_title

Journal of biochemistry

authors

Hashizume S,Honjoh T,Shoji M

doi

10.1093/oxfordjournals.jbchem.a134236

subject

Has Abstract

pub_date

1983-04-01 00:00:00

pages

1109-18

issue

4

eissn

0021-924X

issn

1756-2651

journal_volume

93

pub_type

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