Posttranscriptional autoregulation of Escherichia coli threonyl tRNA synthetase expression in vivo

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.

[1]  M. Grunberg‐Manago,et al.  Autogenous control of Escherichia coli threonyl-tRNA synthetase expression in vivo. , 1985, Journal of molecular biology.

[2]  M. Grunberg‐Manago,et al.  Structural and transcriptional evidence for related thrS and infC expression. , 1983, Proceedings of the National Academy of Sciences of the United States of America.

[3]  M. Springer,et al.  Escherichia coli phenylalanyl-tRNA synthetase operon: characterization of mutations isolated on multicopy plasmids , 1982, Journal of bacteriology.

[4]  M. Springer,et al.  Escherichia coli phenylalanyl-tRNA synthetase operon: transcription studies of wild-type and mutated operons on multicopy plasmids , 1982, Journal of bacteriology.

[5]  J. Hershey,et al.  A sensitive immunoblotting method for measuring protein synthesis initiation factor levels in lysates of Escherichia coli. , 1981, The Journal of biological chemistry.

[6]  P. Schimmel,et al.  An aminoacyl tRNA synthetase binds to a specific DNA sequence and regulates its gene transcription , 1981, Nature.

[7]  M. Grunberg‐Manago,et al.  Physical localisation and cloning of the structural gene for E. coli initiation factor IF3 from a group of genes concerned with translation. , 1980, Gene.

[8]  S. Cohen,et al.  In vitro gene fusions that join an enzymatically active beta-galactosidase segment to amino-terminal fragments of exogenous proteins: Escherichia coli plasmid vectors for the detection and cloning of translational initiation signals , 1980, Journal of bacteriology.

[9]  L. Gold,et al.  Autogenous translational repression of bacteriophage T4 gene 32 expression in vitro. , 1978, Journal of molecular biology.

[10]  A. Böck,et al.  Threonyl-Transfer Ribonucleic Acid Synthetase from Escherichia coli: Subunit Structure and Genetic Analysis of the Structural Gene by Means of a Mutated Enzyme and of a Specialized Transducing Lambda Bacteriophage , 1977, Journal of bacteriology.

[11]  F. Neidhardt,et al.  Chemical measurement of steady-state levels of ten aminoacyl-transfer ribonucleic acid synthetases in Escherichia coli , 1977, Journal of bacteriology.

[12]  I. Saint-Girons,et al.  Threonyl-transfer ribonucleic acid synthetase and the regulation of the threonine operon in Escherichia coli , 1977, Journal of bacteriology.

[13]  F. Neidhardt,et al.  Culture Medium for Enterobacteria , 1974, Journal of bacteriology.

[14]  C. Yanofsky,et al.  Structural Interactions Between Amino Acid Residues at Positions 22 and 211 in the Tryptophan Synthetase Alpha Chain of Escherichia coli , 1974, Journal of bacteriology.

[15]  U. K. Laemmli,et al.  Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4 , 1970, Nature.

[16]  R. Gourse,et al.  Regulation of the synthesis of ribosomes and ribosomal components. , 1984, Annual review of biochemistry.

[17]  D. Botstein,et al.  Advanced bacterial genetics , 1980 .

[18]  Jeffrey H. Miller Experiments in molecular genetics , 1972 .