Posttranscriptional Autoregulation of Escherichia Coli Threonyl TRNA Synthetase Expression in Vivo

Overview

Journal J Bacteriol

Publisher American Society for Microbiology

Specialty Microbiology

Date 1986 Jan 1

PMID 3510186

Citations 15

Authors

J S Butler

M Springer

J DONDON

M GRUNBERG-MANAGO

Affiliations

Soon will be listed here.

Abstract

Five mutations in thrS, the gene for threonyl-tRNA synthetase, have been characterized, and the sites of the mutations have been localized to different regions of the thrS gene by recombination with M13 phage carrying portions of the thrS gene. Quantitative immunoblotting shows that some of these mutations cause the overproduction of structurally altered threonyl-tRNA synthetase in vivo. The amounts of in vivo thrS mRNA as measured by quantitative hybridization are, however, the same as wild-type levels for each mutant. These results demonstrate that the expression of threonyl-tRNA synthetase is autoregulated at the posttranscriptional level in vivo.

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The first step in the functional inactivation of the Escherichia coli polynucleotide phosphorylase messenger is a ribonuclease III processing at the 5' end.

Portier C, DONDON L, GRUNBERG-MANAGO M, Regnier P EMBO J. 1987; 6(7):2165-70.

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