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PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
2007-9-17
pubmed:abstractText
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.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
1438-4221
pubmed:author
pubmed:issnType
Print
pubmed:volume
297
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
451-7
pubmed:meshHeading
pubmed:year
2007
pubmed:articleTitle
Novel biochemical properties of a CRP/FNR family transcription factor from Mycobacterium tuberculosis.
pubmed:affiliation
Laboratory of Molecular and Cellular Biology, CDFD, Hyderabad 500076, India.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't