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pubmed-article:17702648pubmed:abstractTextCyclic AMP (cAMP) receptor protein (CRP)/fumarate nitrate reductase regulator (FNR) family proteins are actively associated with defense against low oxygen stress, starvation and extreme temperature conditions. They are DNA-binding proteins and regulate target genes carrying the regulatory CRP/FNR cognate nucleotide sequence elements. Recombinant protein encoded by the Mycobacterium tuberculosis ORF Rv3676, a putative CRP/FNR regulator, was purified from Escherichia coli and was found to exist as dimer, devoid of any metal cation cofactor. Purified rRv3676 exhibited cAMP binding in a concentration-dependent manner. At lower concentrations of cAMP (6-10 microM) rRv3676 shows positive cooperativity; at 10 microM cAMP the protein exists in the most open conformation. rRv3676 could bind specifically to the putative CRP/FNR nucleotide sequence elements as evident from electrophoretic mobility shift assay.lld:pubmed
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pubmed-article:17702648pubmed:articleTitleNovel biochemical properties of a CRP/FNR family transcription factor from Mycobacterium tuberculosis.lld:pubmed
pubmed-article:17702648pubmed:affiliationLaboratory of Molecular and Cellular Biology, CDFD, Hyderabad 500076, India.lld:pubmed
pubmed-article:17702648pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:17702648pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
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