Redox Proteins of Mycobacterium tuberculosis

Swastik Phulera, Mohd. Akif, Abhijit A Sardesai, Shekhar C Mande

Abstract


Evolution of life took place in a reducing atmosphere. As a reminiscence of this, cytoplasm of all living organisms is reducing in nature. Furthermore most biochemical reactions like energy production etc. are redox in nature requiring either an electron supplier or acceptor. The maintenance of redox state thus becomes extremely crucial for any cell. Cells typically devote considerable resources for the maintenance of their redox state. M. tuberculosis successfully evades an array of host generated redox stresses. For this M. tuberculosis employs a large number of redox sensors and effectors. In our laboratory we have been studying some of these central players with a hope to be able to gain insights into the pathogen. We shall try to discuss the relevance of redox and our efforts to understand the same in this review.

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References


WHO, WHO Global Tuberculosis Report (Geneva: WHO Press, 2013), Pages.

D. Ritz and J. Beckwith, “Roles of thiol-redox pathways in bacteria,” Annual review of microbiology, 55 (2001), 21–48.

D.E. Fomenko and V.N. Gladyshev, “Identity and functions of CxxC-derived motifs,” Biochemistry, 42 (2003), 11214–25.

P.T. Chivers, K.E. Prehoda and R.T. Raines, “The CXXC Motif: A Rheostat in the Active Site,” Biochemistry, 36 (1997), 4061–66.

T. Jaeger, H. Budde, L. Flohe, U. Menge, M. Singh, M. Trujillo and R. Radi, “Multiple thioredoxin-mediated routes to detoxify hydroperoxides in Mycobacterium tuberculosis,” Arch Biochem Biophys, 423 (2004), 182–91.

S.T. Cole, R. Brosch, J. Parkhill, T. Garnier, C. Churcher, D. Harris, S.V. Gordon, K. Eiglmeier, S. Gas, C.E. Barry, 3rd, F. Tekaia, K. Badcock, D. Basham, D. Brown, T. Chillingworth, R. Connor, R. Davies, K. Devlin, T. Feltwell, S. Gentles, N. Hamlin, S. Holroyd, T. Hornsby, K. Jagels, A. Krogh, J. McLean, S. Moule, L. Murphy, K. Oliver, J. Osborne, M.A. Quail, M.A. Rajandream, J. Rogers, S. Rutter, K. Seeger, J. Skelton, R. Squares, S. Squares, J.E. Sulston, K. Taylor, S. Whitehead and B.G. Barrell, “Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence,” Nature, 393 (1998), 537–44.

D.R. Sherman, K. Mdluli, M.J. Hickey, T.M. Arain, S.L. Morris, C.E. Barry, 3rd and C.K. Stover, “Compensatory ahpC gene expression in isoniazid-resistant Mycobacterium tuberculosis,” Science, 272 (1996), 1641–43.

R. Chauhan and S.C. Mande, “Characterization of the Mycobacterium tuberculosis H37Rv alkyl hydroperoxidase AhpC points to the importance of ionic interactions in oligomerization and activity,” Biochem. J., 354 (2001), 209–15.

R. Chauhan and S.C. Mande, “Site-directed mutagenesis reveals a novel catalytic mechanism of Mycobacterium tuberculosis alkylhydroperoxidase C,” Biochem. J., 367 (2002), 255–61.

B.G. Guimaraes, H. Souchon, N. Honore, B. Saint-Joanis, R. Brosch, W. Shepard, S.T. Cole and P.M. Alzari, “Structure and mechanism of the alkyl hydroperoxidase AhpC, a key element of the Mycobacterium tuberculosis defense system against oxidative stress,” J Biol Chem, 280 (2005), 25735–42.

J.L. Martin, “Thioredoxin—a fold for all reasons,” Structure, 3 (1995), 245–50.

H. Kadokura, F. Katzen and J. Beckwith, “Protein disulfide bond formation in prokaryotes,” Annu Rev Biochem, 72 (2003), 111–35.

C.H. Williams, Jr., “Mechanism and structure of thioredoxin reductase from Escherichia coli,” FASEB J, 9 (1995), 1267–76.

G.B. Kallis and A. Holmgren, “Differential reactivity of the functional sulfhydryl groups of cysteine-32 and cysteine-35 present in the reduced form of thioredoxin from Escherichia coli,” Journal of Biological Chemistry, 255 (1980), 10261–65.

M. Akif, G. Khare, A.K. Tyagi, S.C. Mande and A.A. Sardesai, “Functional studies of multiple thioredoxins from Mycobacterium tuberculosis,” J. Bacteriol., 190 (2008), 7087–95.

M. Akif, K. Suhre, C. Verma and S.C. Mande, “Conformational flexibility of Mycobacterium tuberculosis thioredoxin reductase: crystal structure and normal-mode analysis,” Acta Crystallogr. D Biol. Crystallogr., 61 (2005), 1603–11.

P. Nordlund and P. Reichard, “Ribonucleotide reductases,” Annu Rev Biochem, 75 (2006), 681–706.

F. Yang, S.C. Curran, L.S. Li, D. Avarbock, J.D. Graf, M.M. Chua, G. Lu, J. Salem and H. Rubin, “Characterization of two genes encoding the Mycobacterium tuberculosis ribonucleotide reductase small subunit,” J Bacteriol, 179 (1997), 6408–15.

S.S. Dawes, D.F. Warner, L. Tsenova, J. Timm, J.D. McKinney, G. Kaplan, H. Rubin and V. Mizrahi, “Ribonucleotide reduction in Mycobacterium tuberculosis: function and expression of genes encoding class Ib and class II ribonucleotide reductases,” Infect Immun, 71 (2003), 6124–31.

R. Rofougaran, M. Crona, M. Vodnala, B.M. Sjoberg and A. Hofer, “Oligomerization status directs overall activity regulation of the Escherichia coli class Ia ribonucleotide reductase,” J Biol Chem, 283 (2008), 35310–18.

A. Jordan and P. Reichard, “Ribonucleotide reductases,” Annu Rev Biochem, 67 (1998), 71–98.

M. Stehr and Y. Lindqvist, “NrdH-redoxin of Corynebacterium ammoniagenes forms a domain-swapped dimer,” Proteins, 55 (2004), 613–19.

S. Phulera and S.C. Mande, “The crystal structure of Mycobacterium tuberculosis NrdH at 0.87 A suggests a possible mode of its activity,” Biochemistry, 52, 4056–65.


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