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

International Journal of Medical Microbiology

Volumn 297, Issue 6, 2007, Pages 451-457

  Akhter, Yusuf ^a   Tundup, Smanla ^a   Hasnain, Seyed E ^a,b,c,d  

^a CDFD   (India)

^b JAWAHARLAL NEHRU CENTRE FOR ADVANCED SCIENTIFIC RESEARCH   (India)

^c UNIVERSITY OF HYDERABAD   (India)

^d INSTITUTE OF LIFE SCIENCES   (India)

Author keywords

Cyclic AMP; Gene regulation; Hypoxia; Rv3676; Starvation; Transcription factor

Indexed keywords

CYCLIC AMP; CYCLIC AMP BINDING PROTEIN; DNA BINDING PROTEIN; FUMARATE NITRATE REDUCTASE; METAL ION; OXIDOREDUCTASE; RECOMBINANT PROTEIN; TRANSCRIPTION FACTOR; UNCLASSIFIED DRUG;

ARTICLE; CONCENTRATION (PARAMETERS); ESCHERICHIA COLI; GEL MOBILITY SHIFT ASSAY; GENE TARGETING; MYCOBACTERIUM TUBERCULOSIS; NONHUMAN; NUCLEOTIDE SEQUENCE; OPEN READING FRAME; OXIDATIVE STRESS; PROTEIN ANALYSIS; PROTEIN CONFORMATION; PROTEIN FAMILY; PROTEIN PURIFICATION; STARVATION; TEMPERATURE DEPENDENCE;

EID: 34548504822     PISSN: 14384221     EISSN: 16180607     Source Type: Journal    
DOI: 10.1016/j.ijmm.2007.04.009     Document Type: Article

References (19)

1. Akif M., Akhter Y., Hasnain S.E., and Mande S.C. Crystallization and preliminary X-ray crystallographic studies of Mycobacterium tuberculosis CRP/FNR family transcriptional regulator. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 62 (2006) 873-875
2. Bai G., McCue L.A., and McDonough K.A. Characterization of Mycobacterium tuberculosis Rv3676 (CRPMt), a cyclic AMP receptor protein-like DNA binding protein. J. Bacteriol. 187 (2005) 7795-7804
3. Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72 (1976) 248-254
4. Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C., Harris D., Gordon S.V., Eiglmeier K., Gas S., Barry III C.E., Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T., Connor R., Davies R., Devlin K., Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S., Murphy L., Oliver K., Osborne J., Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton J., Squares R., Squares S., Sulston J.E., Taylor K., Whitehead S., and Barrell B.G. Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence. Nature 393 (1998) 537-544
5. Gazdik M.A., and McDonough K.A. Identification of cyclic AMP-regulated genes in Mycobacterium tuberculosis complex bacteria under low-oxygen conditions. J. Bacteriol. 187 (2005) 2681-2692
6. Green J., Scott C., and Guest J. Functional versatility in the CRP-FNR superfamily of transcription factors: FNR and FLP. Adv. Microb. Physiol. 44 (2001) 1-34
7. Kolb A., Busby S., Garges S., and Adhya S. Transcriptional regulation by cAMP and its receptor protein. Annu. Rev. Biochem. 62 (1993) 749-795
8. Korner H., Sofia H.J., and Zumft W.G. Phylogeny of the bacterial superfamily of CRP-FNR transcription regulators: exploiting the metabolic spectrum by controlling alternative gene programs. FEMS Microbiol. Rev. 27 (2003) 559-592
9. Lambden P.R., and Guest J.R. Mutants of Escherichia coli K12 unable to use fumarate as an anerobic electron acceptor. J. Gen. Microbiol. 97 (1976) 145-160
10. Lanzilotta W.N., Schuller D.J., Thorsteinsson M.V., Kerby R.L., Roberts G.P., and Poulos T.L. Structure of the CO sensing transcription activator CooA. Nat. Struct. Biol. 7 (2000) 876-880
11. Mesa S., Bedmar E.J., Chanfon A., Hauke H., and Fischer H. Bradyrhizobium japonicum NnrR, a denitrification regulator, expands the FixLJ-FixK2 regulatory cascade. J. Bacteriol. 185 (2003) 3978-3982
12. Prakash P., Yellaboina S., Ranjan A., and Hasnain S.E. Computational prediction and experimental verification of novel IdeR binding sites in the upstream sequences of Mycobacterium tuberculosis ORFs. Bioinformatics 21 (2005) 2161-2166
13. Rickman L., Scott C., Hunt D.M., Hutchinson T., Menéndez M.C., Whalan R., Hinds J., Colston M.J., Green J., and Buxton R.S. A member of the cAMP receptor protein family of transcription regulators in Mycobacterium tuberculosis is required for virulence in mice and controls transcription of the rpfA gene coding for a resuscitation promoting factor. Mol. Microbiol. 56 (2005) 1274-1286
14. Schultz S.C., Shields G.C., and Steitz T.A. Crystal structure of a CAP-DNA complex: the DNA is bent by 90 degrees. Science 253 (1991) 1001-1007
15. Spreadbury C.L., Pallen M.J., Overton T., Behr M.A., Mostowy S., Spiro S., Busby S.J., and Cole J.A. Point mutations in the DNA- and cNMP-binding domains of the homologue of the cAMP receptor protein (CRP) in Mycobacterium bovis BCG: implications for the inactivation of a global regulator and strain attenuation. Microbiology 151 (2005) 547-556
16. Ulrichs T., and Kaufmann S.H. New insights into the function of granulomas in human tuberculosis. J. Pathol. 208 (2006) 261-269
17. Vollack K., Hartig E., Korner H., and Zumft W.G. Multiple transcription factors of the FNR family in denitrifying Pseudomonas stutzeri: characterization of four fnr-like genes, regulatory responses and cognate metabolic processes. Mol. Microbiol. 31 (1999) 1681-1694
18. World Health Organization. Tuberculosis Fact Sheet No. 104 - Global and Regional Incidence (2006), World Health Organization, Geneva
19. Yang J.T., Wu C.S., and Martinez H.M. Calculation of protein conformation from circular dichroism. Methods Enzymol. 130 (1986) 208-269