Mycobacterium tuberculosis mtrA merodiploid strains with point mutations in the signal-receiving domain of MtrA exhibit growth defects in nutrient broth

Plasmid

Volumn 65, Issue 3, 2011, Pages 210-218

  Al Zayer, Maha ^a   Stankowska, Dorota ^a   Dziedzic, Renata ^a   Sarva, Krishna ^a   Madiraju, Murty V ^a   Rajagopalan, Malini ^a  

^a UNIVERSITY OF TEXAS HEALTH CENTER   (United States)

Author keywords

Merodiploids; Mutants; Mycobacterium tuberculosis; Real time PCR; Response regulator; Signal transduction

Indexed keywords

BACTERIAL ANTIGEN; BACTERIAL PROTEIN; FBPB PROTEIN; MICROORGANISM PROTEIN; MTRA PROTEIN; MTRB PROTEIN; UNCLASSIFIED DRUG;

AMINO ACID SUBSTITUTION; ARTICLE; AUTOPHOSPHORYLATION; BACTERIAL GROWTH; BACTERIAL STRAIN; BACTERIUM CULTURE; CONTROLLED STUDY; MYCOBACTERIUM TUBERCULOSIS; NONHUMAN; PHENOTYPE; PROMOTER REGION; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN INTERACTION; PROTEIN PROTEIN INTERACTION; PROTEIN SYNTHESIS; SIGNAL TRANSDUCTION; WILD TYPE;

ACYLTRANSFERASES; AMINO ACIDS; ANTIGENS, BACTERIAL; ATP-BINDING CASSETTE TRANSPORTERS; BACTERIAL PROTEINS; GENE EXPRESSION REGULATION, BACTERIAL; MYCOBACTERIUM TUBERCULOSIS; PHOSPHORYLATION; POINT MUTATION; PROMOTER REGIONS, GENETIC; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; RNA-BINDING PROTEINS; SIGNAL TRANSDUCTION; TRANSCRIPTION FACTORS;

BACTERIA (MICROORGANISMS); MYCOBACTERIUM TUBERCULOSIS;

EID: 79954424328     PISSN: 0147619X     EISSN: 10959890     Source Type: Journal    
DOI: 10.1016/j.plasmid.2011.01.002     Document Type: Article

References (22)

1. Aravind L., Ponting C.P. The cytoplasmic helical linker domain of receptor histidine kinase and methyl-accepting proteins is common to many prokaryotic signalling proteins. FEMS Microbiol. Lett. 1999, 176:111-116.
2. Bilwes A.M., et al. Structure of CheA, a signal-transducing histidine kinase. Cell 1999, 96:131-141.
3. Cangelosi G.A., et al. The two-component regulatory system mtrAB is required for morphotypic multidrug resistance in Mycobacterium avium. Antimicrob. Agents Chemother. 2006, 50:461-468.
4. Cole S.T., et al. Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence. Nature 1998, 393:537-544.
5. Domian I.J., et al. Cell type-specific phosphorylation and proteolysis of a transcriptional regulator controls the G1-to-S transition in a bacterial cell cycle. Cell 1997, 90:415-424.
6. Fol M., et al. Modulation of Mycobacterium tuberculosis proliferation by MtrA, an essential two-component response regulator. Mol. Microbiol. 2006, 60:643-657.
7. Friedland N., et al. Domain orientation in the inactive response regulator Mycobacterium tuberculosis MtrA provides a barrier to activation. Biochemistry 2007, 46:6733-6743.
8. Hoch J.A. Two component and phosphorely signal transduction. Curr. Opin. Microbiol. 2000, 3:165-170.
9. Karimova G., et al. Interaction network among Escherichia coli membrane proteins involved in cell division as revealed by bacterial two-hybrid analysis. J. Bacteriol. 2005, 187:2233-2243.
10. Klose K.E., et al. Glutamate at the site of phosphorylation of nitrogen-regulatory protein NTRC mimics aspartyl-phosphate and activates the protein. J. Mol. Biol. 1993, 232:67-78.
11. Lan C.Y., Igo M.M. Differential expression of the OmpF and OmpC porin proteins in Escherichia coli K-12 depends upon the level of active OmpR. J. Bacteriol. 1998, 180:171-174.
12. Li Y., et al. The characterization of conserved binding motifs and potential target genes for M. tuberculosis MtrAB reveals a link between the two-component system and the drug resistance of M. smegmatis. BMC Microbiol. 2010, 10:242.
13. Moker N., et al. Deletion of the genes encoding the MtrA-MtrB two-component system of Corynebacterium glutamicum has a strong influence on cell morphology, antibiotics susceptibility and expression of genes involved in osmoprotection. Mol. Microbiol. 2004, 54:420-438.
14. Moker N., et al. In vitro analysis of the two-component system MtrB-MtrA from Corynebacterium glutamicum. J. Bacteriol. 2007, 189:3645-3649.
15. Nair N., et al. Synchronous replication initiation in novel Mycobacterium tuberculosis dnaA cold-sensitive mutants. Mol. Microbiol. 2009, 71:291-304.
16. Nguyen H.T., et al. A lipoprotein modulates activity of the MtrAB two-component system to provide intrinsic multidrug resistance, cytokinetic control and cell wall homeostasis in Mycobacterium. Mol. Microbiol. 2010, 76:348-364.
17. Rajagopalan M., et al. Mycobacterium tuberculosis origin of replication and the promoter for immunodominant secreted antigen 85B are the targets of MtrA, the essential response regulator. J. Biol. Chem. 2010, 285:15816-15827.
18. Stock A.M., et al. Two-component signal transduction. Annu. Rev. Biochem. 2000, 69:183-215.
19. Via L.E., et al. Elements of signal transduction in Mycobacterium tuberculosis: in vitro phosphorylation and in vivo expression of the response regulator MtrA. J. Bacteriol. 1996, 178:3314-3321.
20. Wagner D., et al. Elemental analysis of Mycobacterium avium-, Mycobacterium tuberculosis-, and Mycobacterium smegmatis-containing phagosomes indicates pathogen-induced microenvironments within the host cell's endosomal system. J. Immunol. 2005, 174:1491-1500.
21. Wagner D., et al. Changes of the phagosomal elemental concentrations by Mycobacterium tuberculosis Mramp. Microbiology 2005, 151:323-332.
22. Zahrt T.C., Deretic V. An essential two-component signal transduction system in Mycobacterium tuberculosis. J. Bacteriol. 2000, 182:3832-3838.