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PMID: 6094549 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Structure and autoregulation of the metJ regulatory gene in Escherichia coli.

The Journal of biological chemistry ·Vol. 259 ·No. 22 ·1984-11-25 ·Pages 14282-5

Saint-Girons I, Duchange N, Cohen GN, Zakin MM

Abstract

The nucleotide sequence of the Escherichia coli metJ regulatory gene (312 nucleotides) has been determined as well as that of two mutations located within the gene. Analysis of the sequence downstream from the metJ gene has revealed inverted repeats homologous to several intercistronic regions, also reported to occur between operons. A hybrid protein that contains the 55 first amino acid residues of the metJ protein substituting for the 8 amino acid residues at the NH2 terminus of beta-galactosidase was produced by gene fusion. The hybrid protein retaining beta-galactosidase activity was purified. Its amino-terminal sequence was determined and this allowed us to locate the translational start codon of the metJ gene. Evidence was provided for autoregulation by repression of the metJ gene. By sequencing upstream from metJ, the region situated between the metJ and metB genes was found to contain putative operator structures that we propose to call "Met boxes."

MeSH Terms
Alleles Amino Acid Sequence Bacterial Proteins/analysis Base Sequence Chromosome Inversion DNA, Bacterial/analysis Escherichia coli/genetics Genes, Regulator Homeostasis Repetitive Sequences, Nucleic Acid beta-Galactosidase/genetics
Chemicals
Bacterial Proteins DNA, Bacterial beta-Galactosidase
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Saint-Girons I
Duchange N
Cohen G N
Zakin M M
Article Info
Journal
The Journal of biological chemistry
Abbr.
J Biol Chem
ISSN
0021-9258
Published
1984-11-25
Pages
14282-5
Language
English
Region
United States
NLM ID
2985121R
Subset
IM
Databases
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