Novel biochemical properties of a CRP/FNR family transcription factor from Mycobacterium tuberculosis

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...

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Bibliographic Details
Published in:International journal of medical microbiology 2007-10, Vol.297 (6), p.451-457
Main Authors: Akhter, Yusuf, Tundup, Smanla, Hasnain, Seyed E
Format: Article
Language:English
Subjects:
Bacterial Proteins - chemistry
Bacterial Proteins - genetics
Bacterial Proteins - isolation & purification
Bacterial Proteins - metabolism
Binding Sites
Coenzymes - analysis
Cyclic AMP
Cyclic AMP - metabolism
Dimerization
DNA, Bacterial - metabolism
Electrophoretic Mobility Shift Assay
Escherichia coli
Escherichia coli - genetics
Gene regulation
Hypoxia
Infectious Disease
Medical Education
Metals - analysis
Mycobacterium tuberculosis
Mycobacterium tuberculosis - physiology
Protein Binding
Protein Conformation
Recombinant Proteins - chemistry
Recombinant Proteins - genetics
Recombinant Proteins - isolation & purification
Recombinant Proteins - metabolism
Rv3676
Starvation
Transcription factor
Transcription Factors - chemistry
Transcription Factors - genetics
Transcription Factors - isolation & purification
Transcription Factors - metabolism
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Summary: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 μM) rRv3676 shows positive cooperativity; at 10 μM 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.
ISSN:1438-4221
1618-0607
DOI:10.1016/j.ijmm.2007.04.009