Akhter, Y. and Tundup, S. and Hasnain, S.E. (2007) Novel biochemical properties of a CRP/FNR family transcription factor from Mycobacterium tuberculosis. International Journal of Medical Microbiology, 297 (6). pp. 451-457. ISSN 1438-4221

Text Int J Med Microbiol 297 p451.pdf Restricted to Repository staff only Download (384Kb) | Request a copy

Abstract

Cyclic 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.

Item Type:	Article
Depositing User:	Users 2 not found.
Date Deposited:	13 Aug 2015 10:51
Last Modified:	13 Aug 2015 10:52
URI:	http://cdfd.sciencecentral.in/id/eprint/329

Actions (login required)

View Item