Linked Life Data

10452892

Source:http://linkedlifedata.com/resource/pubmed/id/10452892

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pubmed-article:10452892pubmed:abstractTextRecently the crystal structure of the DNA-unbound form of the full-length hexameric Bacillus stearothermophilus arginine repressor (ArgR) has been resolved, providing a possible explanation for the mechanism of arginine-mediated repressor-operator DNA recognition. In this study we tested some of these functional predictions by performing site-directed mutagenesis of distinct amino acid residues located in two regions, the N-terminal DNA-binding domain and the C-terminal oligomerization domain of ArgR. A total of 15 mutants were probed for their capacity to repress the expression of the reporter argC - lacZ gene fusion in Escherichia coli cells. Substitutions of highly conserved amino acid residues in the alpha2 and alpha3 helices, located in the winged helix-turn-helix DNA-binding motif, reduced repression. Loss of DNA-binding capacity was confirmed in vitro for the Ser42Pro mutant which showed the most pronounced effect in vivo. In E. coli, the wild-type B. stearothermophilus ArgR molecule behaves as a super-repressor, since recombinant E. coli host cells bearing B. stearothermophilusargR on a multicopy vector did not grow in selective minimal medium devoid of arginine and grew, albeit weakly, when l -arginine was supplied. All mutants affected in the DNA-binding domain lost this super-repressor behaviour. Replacements of conserved leucine residues at positions 87 and/or 94 in the C-terminal domain by other hydrophobic amino acid residues proved neutral or caused either derepression or stronger super-repression. Substitution of Leu87 by phenylalanine was found to increase the DNA-binding affinity and the protein solubility in the context of a double Leu87Phe/Leu94Val mutant. Structural modifications occasioned by the various amino acid substitutions were confirmed by circular dichroism analysis and structure modelling.lld:pubmed
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pubmed-article:10452892pubmed:authorpubmed-author:TakahashiMMlld:pubmed
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pubmed-article:10452892pubmed:copyrightInfoCopyright 1999 Academic Press.lld:pubmed
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pubmed-article:10452892pubmed:year1999lld:pubmed
pubmed-article:10452892pubmed:articleTitleMutational analysis of the thermostable arginine repressor from Bacillus stearothermophilus: dissecting residues involved in DNA binding properties.lld:pubmed
pubmed-article:10452892pubmed:affiliationLaboratoire de Biotechnologie, UPRES Biocatalyse, Faculté des Sciences et des Techniques, Université de Nantes, Nantes, Cedex 3, 44322, France.lld:pubmed
pubmed-article:10452892pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:10452892pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
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