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- Title
Mutant Escherichia coli arginine repressor proteins that fail to bind L--arginine, yet retain the ability to bind their normal DNA--binding sites.
- Authors
Burke, Mary; Merican, Amir F.; Sherratt, David J.
- Abstract
The <em>Escherichia coli</em> arginine repressor (ArgR) is an L-arginine-dependent DNA-binding protein that controls expression of the arginine biosynthetic genes and is required as an accessory protein in Xer site-specific recombination at <em>cer</em> and related recombination sites in plasmids. Site-directed mutagenesis was used to isolate two mutants of <em>E. coli</em> ArgR that were defective in arginine binding. Results from <em>in vivo</em> and <em>in vitro</em> experiments demonstrate that these mutants stili act as repressors and bind their specific DNA sequences in an arginine-independent manner. Both mutants support Xer site-specific recombination at <em>cer</em>. One of the mutant proteins was purified and shown to bind to its DNA target sequences <em>in vitro</em> with different affinity and as a different molecular species to wild-type ArgR.
- Subjects
ESCHERICHIA coli; ESCHERICHIA; ARGININE; AMINO acids; ORGANIC acids; IMINO acids; DNA-binding proteins; PROTEINS; PLASMIDS
- Publication
Molecular Microbiology, 1994, Vol 13, Issue 4, p609
- ISSN
0950-382X
- Publication type
Article
- DOI
10.1111/j.1365-2958.1994.tb00455.x