Integral role of the I'-helix in the function of the "inactive" C-terminal domain of catalase-peroxidase (KatG)

Biochimica et Biophysica Acta - Proteins and Proteomics

Volumn 1834, Issue 1, 2013, Pages 362-371

  Wang, Yu ^a   Goodwin, Douglas C ^a  

^a AUBURN UNIVERSITY   (United States)

Author keywords

Catalase; Folding platform; Gene duplication; KatG; Peroxidase

Indexed keywords

HEME; KATG PROTEIN;

AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CONFORMATION; DNA HELIX; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME MECHANISM; LOSS OF FUNCTION MUTATION; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN STRUCTURE; SPECTROSCOPY;

AMINO ACID SUBSTITUTION; CATALASE; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; MUTATION, MISSENSE; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY;

EID: 84871718518     PISSN: 15709639     EISSN: 18781454     Source Type: Journal    
DOI: 10.1016/j.bbapap.2012.08.003     Document Type: Article

References (43)

1. Y. Zhang, B. Heym, B. Allen, D. Young, and S. Cole The catalase-peroxidase gene and isoniazid resistance of Mycobacterium tuberculosis Nature 358 1992 591 593
2. S. Chouchane, I. Lippai, and R.S. Magliozzo Catalase-peroxidase (Mycobacterium tuberculosis KatG) catalysis and isoniazid activation Biochemistry 39 2000 9975 9983
3. B. Lei, C.J. Wei, and S.C. Tu Action mechanism of antitubercular isoniazid. Activation by Mycobacterium tuberculosis KatG, isolation, and characterization of InhA inhibitor J. Biol. Chem. 275 2000 2520 2526
4. E. Garcia, Y.A. Nedialkov, J. Elliott, V.L. Motin, and R.R. Brubaker Molecular characterization of KatY (antigen 5), a thermoregulated chromosomally encoded catalase-peroxidase of Yersinia pestis J. Bacteriol. 181 1999 3114 3122
5. R.J. Mehigh, and R.R. Braubaker Major stable peptides of Yersinia pestis synthesized during the low-calcium response Infect. Immun. 61 1993 13 22
6. B.A. Chromy, M.W. Choi, G.A. Murphy, A.D. Gonzales, C.H. Corzett, B.C. Chang, J.P. Fitch, and S.L. McCutchen-Maloney Proteomic characterization of Yersinia pestis virulence J. Bacteriol. 187 2005 8172 8180
7. P. Bandyopadhyay, B. Byrne, Y. Chan, M.S. Swanson, and H.M. Steinman Legionella pneumophila catalase-peroxidases are required for proper trafficking and growth in primary macrophages Infect. Immun. 71 2003 4526 4535
8. M. Zamocky, and C. Obinger Molecular phylogeny of heme peroxidases M. Ayala, E. Torres, Biocatalysis Based on Heme Peroxidases 2010 Springer-Verlag Berlin 7 35
9. J.A. Imlay Cellular defenses against superoxide and hydrogen peroxide Annu. Rev. Biochem. 77 2008 755 776
10. P.C. Loewen Bacterial catalases Oxidative Stress and the Molecular Biology of Antioxidant Defenses 1997 Cold Spring Harbor Laboratory Press New York
11. K.G. Welinder Bacterial catalase-peroxidases are gene duplicated members of the plant peroxidase superfamily Biochim. Biophys. Acta 1080 1991 215 220
12. Y. Yamada, T. Fujiwara, T. Sato, N. Igarashi, and N. Tanaka The 2.0 angstrom crystal structure of catalase-peroxidase from Haloarcula marismortui Nat. Struct. Biol. 9 2002 691 695
13. K. Wada, T. Tada, Y. Nakamura, T. Kinoshita, M. Tamoi, S. Shigeoka, and K. Nishimura Crystallization and preliminary X-ray diffraction studies of catalase-peroxidase from Synechococcus PCC 7942 Acta Crystallogr. D Biol. Crystallogr. 58 2002 157 159
14. X. Carpena, S. Loprasert, S. Mongkolsuk, J. Switala, P.C. Loewen, and I. Fita Catalase-peroxidase KatG of Burkholderia pseudomallei at 1.7 A resolution J. Mol. Biol. 327 2003 475 489
15. T. Bertrand, N.A.J. Eady, J.N. Jones, J.M. Nagy, B. Jamart-Gregoire, E.L. Raven, and K.A. Brown Crystal structure of Mycobacterium tuberculosis catalase-peroxidase J. Biol. Chem. 279 2004 38991 38999
16. M. Zamocky, G. Regelsberger, C. Jakopitsch, and C. Obinger The molecular peculiarities of catalase-peroxidases FEBS Lett. 492 2001 177 182
17. S.W. Yu, S. Girotto, X.B. Zhao, and R.S. Magliozzo Rapid formation of Compound II and a tyrosyl radical in the Y229F mutant of Mycobacterium tuberculosis catalase-peroxidase disrupts catalase but not peroxidase function J. Biol. Chem. 278 2003 44121 44127
18. C. Jakopitsch, M. Auer, A. Ivancich, F. Ruker, P.G. Furtmuller, and C. Obinger Total conversion of bifunctional catalase-peroxidase (KatG) to monofunctional peroxidase by exchange of a conserved distal side tyrosine J. Biol. Chem. 278 2003 20185 20191
19. L.J. Donald, O.V. Krokhin, H.W. Duckworth, B. Wiseman, T. Deemagarn, R. Singh, J. Switala, X. Carpena, I. Fita, and P.C. Loewen Characterization of the catalase-peroxidase KatG from Burkholderia pseudomallei by mass spectrometry J. Biol. Chem. 278 2003 35687 35692
20. Y. Li, and D.C. Goodwin Vital roles of an interhelical insertion in catalase-peroxidase bifunctionality Biochem. Biophys. Res. Commun. 318 2004 970 976
21. R.A. Ghiladi, G.M. Knudsen, K.F. Medzihradszky, and P.R. Ortiz de Montellano The Met-Tyr-Trp cross-link in Mycobacterium tuberculosis catalase-peroxidase (KatG): autocatalytic formation and effect on enzyme catalysis and spectroscopic properties J. Biol. Chem. 280 2005 22651 22663
22. S. Banerjee, M. Zamocky, P.G. Furtmuller, and C. Obinger Probing the two-domain structure of homodimeric prokaryotic and eukaryotic catalase-peroxidases Biochim. Biophys. Acta 1804 2010 2136 2145
23. X. Carpena, W. Melik-Adamyan, P.C. Loewen, and I. Fita Structure of the C-terminal domain of the catalase-peroxidase KatG from Escherichia coli Acta Crystallogr. D Biol. Crystallogr. 60 2004 1824 1832
24. M. Zamocky, P.G. Furtmuller, and C. Obinger Evolution of structure and function of Class I peroxidases Arch. Biochem. Biophys. 500 2010 45 57
25. R.D. Baker, C.O. Cook, and D.C. Goodwin Properties of catalase-peroxidase lacking its C-terminal domain Biochem. Biophys. Res. Commun. 320 2004 833 839
26. R.D. Baker, C.O. Cook, and D.C. Goodwin Catalase-peroxidase active site restructuring by a distant and "inactive" domain Biochemistry 45 2006 7113 7121
27. S. Moore 'Round-the-horn site-directed mutagenesis - OpenWetWare http://openwetware.org/wiki/'Round-the-horn-site-directed-mutagenesis Accessed January 2008
28. C.L. Varnado, K.M. Hertwig, R. Thomas, J.K. Roberts, and D.C. Goodwin Properties of a novel periplasmic catalase-peroxidase from Escherichia coli O157:H7 Arch. Biochem. Biophys. 421 2004 166 174
29. S.C. Gill, and P.H. von Hippel Calculation of protein extinction coefficients from amino acid sequence data Anal. Biochem. 182 1989 319 326
30. J.K. Falk K.M. Smith, Porphyrins and Metalloporphyrins 1964 Elsevier Publishing New York 804 807
31. S.L. Scott, W.J. Chen, A. Bakac, and J.H. Espenson Spectroscopic parameters, electrode-potentials, acid ionization-constants, and electron-exchange rates of the 2,2′-azinobis(3-ethylbenzothiazoline-6- sulfonate) radicals and ions J. Phys. Chem.-US 97 1993 6710 6714
32. 2 solutions in UV) Anal. Biochem. 49 1972 474 478
33. A. Fersht Structure and Mechanism in Protein Science: a Guide to Enzyme Catalysis and Protein Folding 1999 W.H. Freeman and Company New York
34. W.R. Hagen Biomolecular EPR Spectroscopy 2009 CRC Press Boca Raton, FL
35. W.R. Hagen TU Delft: Biomolecular EPR Spectroscopy http://www.bt.tudelft. nl/biomolecularEPRspectroscopy 2012
36. C. Zentz, S. Pin, and B. Alpert Stationary and time-resolved circular-dichroism of hemoglobins Methods Enzymol. 232 1994 247 266
37. S.E. Jackson, and A.R. Fersht Folding of chymotrypsin inhibitor-2.1. evidence for a 2-state transition Biochemistry 30 1991 10428 10435
38. G. Tsaprailis, D.W.S. Chan, and A.M. English Conformational states in denaturants of cytochrome C and horseradish peroxidases examined by fluorescence and circular dichroism Biochemistry 37 1998 2004 2016
39. A. Ivancich, C. Jakopitsch, M. Auer, S. Un, and C. Obinger Protein-based radicals in the catalase-peroxidase of Synechocystis PCC6803: a multifrequency EPR investigation of wild-type and variants on the environment of the heme active site J. Am. Chem. Soc. 125 2003 14093 14102
40. S. Chouchane, S. Girotto, S. Kapetanaki, J.P. Schelvis, S. Yu, and R.S. Magliozzo Analysis of heme structural heterogeneity in Mycobacterium tuberculosis catalase-peroxidase (KatG) J. Biol. Chem. 278 2003 8154 8162
41. D.A. Svistunenko, J.A. Worrall, S.B. Chugh, S.C. Haigh, R.A. Ghiladi, and P. Nicholls Ferric haem forms of Mycobacterium tuberculosis catalase-peroxidase probed by EPR spectroscopy: their stability and interplay with pH Biochimie 94 2012 1274 1280
42. G.R. Sutherland, and S.D. Aust The effects of calcium on the thermal stability and activity of manganese peroxidase Arch. Biochem. Biophys. 332 1996 128 134
43. M. Sundaramoorthy, K. Kishi, M.H. Gold, and T.L. Poulos The crystal structure of manganese peroxidase from Phanerochaete chrysosporium at 2.06 - a resolution J. Biol. Chem. 269 1994 32759 32767