Expression of catabolite-sensitive operons in mutants devoid of HPr (a component of the glucose transport system) is severely repressed. ptsH mutants do not utilize substrates of the phosphoenolpyruvate: carbohydrate system (PTS) and many other sugars. Analysis of mutations suppressing the effect of the delta ptsH mutation revealed a new class of reversions which restore the growth of bacteria on different substrates. This mutation (named ptsS) intensifies the growth rate of ptsH mutants and increases the differential rate of beta-galactosidase production. ptsS mutation was mapped in the region of ptsF gene (coding for the fructose specific enzyme II of the PTS) on the 46th min. of the E. coli chromosome map. The effect of the ptsS mutation on the expression of catabolite-sensitive operons manifests only in the presence of the intact enzyme I of the PTS.
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J Antibiot (Tokyo)
March 2008
Department of Cell Membrane Biology, Institute of Scientific and Industrial Research, Osaka University, Ibaraki, Osaka, Japan.
Multidrug efflux pumps contribute to the resistance of Escherichia coli against many antibiotics and biocides. Here, we report that the CRP regulator modulates multidrug resistance in E. coli through repression of the genes encoding the MdtEF multidrug efflux pump.
View Article and Find Full Text PDFArch Biochem Biophys
September 2006
Department of Chemistry and Biochemistry, Texas Tech University, Lubbock, TX 79409, USA.
Expression of catabolite-sensitive operons in Escherichia coli is cAMP-dependent and mediated through the CRP:cAMP complex binding to specific sequences in DNA. Five specific ionic or polar interactions occur in cAMP binding pocket of CRP. E72 interacts with the cAMP 2' OH, R82 and S83 interact with the negatively charged phosphate moiety, and T127 and S128 interact with the adenine ring.
View Article and Find Full Text PDFBiochemistry
August 1995
Department of Human Biological Chemistry and Genetics, University of Texas Medical Branch at Galveston 77555, USA.
Upon activation by cAMP, Escherichia coli cAMP receptor protein (CRP) controls the expression of a network of catabolite sensitive genes. The activation of CRP by cAMP involves conformational changes such as realignments between subunits and domains within the protein. To understand the molecular events that lead to the activation of CRP, point mutations at position 128 were introduced via site-directed mutagenesis in an attempt to specifically affect the subunit interfacial interactions, as well as the ligand-binding reaction.
View Article and Find Full Text PDFJ Biol Chem
December 1994
Department of Human Biological Chemistry and Genetics, University of Texas Medical Branch, Galveston 77555-1055.
cAMP receptor protein (CRP), when interacting with cAMP, controls the expression of a network of catabolite-sensitive genes in Escherichia coli. To understand the molecular events that lead to the activation of CRP, a combined approach of site-directed mutagenesis and thermodynamic analysis was employed to study a member of a specific class of CRP mutant, CRP, which activates the in vivo expression of CRP-dependent operons in cya- strains in the absence of exogenous cAMP. Results from in vitro studies show that the CRP mutant G141Q absolutely requires cAMP for interacting with specific DNA.
View Article and Find Full Text PDFBiochemistry
August 1993
Department of Human Biological Chemistry and Genetics, University of Texas Medical Branch, Galveston 77550.
Escherichia coli cAMP receptor protein (CRP) regulates the expression of a large number of catabolite-sensitive genes. The mechanism of CRP regulation most likely involves communication between subunits and domains. A specific message, such as the activation of CRP, may be manifested as a change in the interactions between these structural entities.
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