Characterization of a large subunit catalase truncated by proteolytic cleavage

Biochemistry

Volumn 44, Issue 15, 2005, Pages 5597-5605

  Chelikani, Prashen ^a   Carpena, Xavier ^a   Perez Luque, Rosa ^b   Donald, Lynda J ^a   Duckworth, Harry W ^a   Switala, Jacek ^a   Fita, Ignacio ^b   Loewen, Peter C ^a  

^a UNIVERSITY OF MANITOBA   (Canada)

^b CSIC   (Spain)

Author keywords

[No Author keywords available]

Indexed keywords

AROMATIC COMPOUNDS; CRYSTAL STRUCTURE; ESCHERICHIA COLI; HYDROGEN PEROXIDE; MASS SPECTROMETRY;

AMINOTRIAZOLE; QUATERNARY STRUCTURE; TERMINAL RESIDUES; TRUNCATION;

ENZYMES;

AMINOTRIAZOLE; AZIDE; CATALASE; PROTEIN SUBUNIT;

ACCURACY; AMINO TERMINAL SEQUENCE; ARTICLE; BINDING AFFINITY; CARBOXY TERMINAL SEQUENCE; CONCENTRATION RESPONSE; CONTROLLED STUDY; CRYSTAL STRUCTURE; DEGRADATION KINETICS; ENZYME ACTIVE SITE; ESCHERICHIA COLI; FRAGMENTATION REACTION; GENETIC HETEROGENEITY; MASS SPECTROMETRY; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN DOMAIN; SENSITIVITY ANALYSIS; SEQUENCE ANALYSIS; SPECTRAL SENSITIVITY; STRUCTURE ANALYSIS;

BINDING SITES; CATALASE; CATALYTIC DOMAIN; CRYSTALLOGRAPHY, X-RAY; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; HEME; HYDROGEN PEROXIDE; KINETICS; MODELS, MOLECULAR; PEPTIDE FRAGMENTS; PEPTIDE HYDROLASES; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, TERTIARY; PROTEIN SUBUNITS; SPECTROMETRY, MASS, ELECTROSPRAY IONIZATION; VARIATION (GENETICS);

ESCHERICHIA COLI;

EID: 17144396321     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi047277m     Document Type: Article

References (45)

1. Nicholls, P., Fita, I., and Loewen, P. C. (2001) Enzymology and structure of catalases, Adv. Inorg. Chem. 51, 51-106.
2. Klotz, M. G., Klassen, G. R., and Loewen, P. C. (1997) Phylogenetic relationships among prokaryotic and eukaryotic catalases, Mol. Biol. Evol. 14, 951.
3. Klotz, M. G., and Loewen, P. C. (2003) The molecular evolution of catalatic hydroperoxidases: Evidence for multiple lateral transfer of genes between prokaryota and from bacteria into eukaryota, Mol. Biol. Evol. 20, 1098-1112.
4. Murthy, M. R. N., Reid, T. J., Sicignano, A., Tanaka, N., and Rossmann, M. G. (1981) Structure of beef liver catalase, J. Mol. Biol. 152, 465-499.
5. Fita, I., Silva, A. M., Murthy, M. R. N., and Rossmann, M. G. (1986) The refined structure of beef liver catalase at 2.5 Å resolution, Acta Crystallogr. B42, 497-515.
6. Vainshtein, B. K., Melik-Adamyan, W. R., Barynin, V. V., Vagin, A. A., and Grebenko, A. I. (1981) Three-dimensional structure of the enzyme catalase, Nature 293, 411-412.
7. Vainshtein, B. K., Melik-Adamyan, W. R., Barynin, V. V., Vagin, A. A., Grebenko, A. I., Borisov, V. V., Bartels, K. S., Fita, I., and Rossmann, M. G. (1986) Three-dimensional structure of catalase from Penicillium vitale, at 2.0 Å resolution, J. Mol. Biol. 188, 49-61.
8. Murshudov, G. N., Melik-Adamyan, W. R., Grebenko, A. I., Barynin, V. V., Vagin, A. A., Vainshtein, B. K., Dauter, Z., and Wilson, K. (1982) Three-dimensional structure of catalase from Micrococcus lysodeikticus at 1.5 Å resolution, FEBS Lett. 312, 127-131.
9. Gouet, P., Jouve, H. M., and Dideberg, O. (1995) Crystal structure of Proteus mirabilis PR catalase with and without bound NADPH, J. Mol. Biol. 249, 933-954.
10. Bravo, J., Verdaguer, N., Tormo, J., Betzel, C., Switala, J., Loewen, P. C., and Fita, I. (1995) Crystal structure of catalase HPII from Escherichia coli, Structure 3, 491-502.
11. Bravo, J., Maté, M. J., Schneider, T., Switala, J., Wilson, K., Loewen, P. C., and Fita, I. (1999) Structure of catalase HPII from Escherichia coli at 1.9 Å resolution, Proteins 34, 155-166.
12. Berthet. S., Nykyri, L., Bravo, J., Maté, M. J., Berthet-Colominas, C., Alzari, P. M., Koller, F., and Fita, I. (1997) Crystallization and preliminary structural analysis of catalase-A from Saccharomyces cerevisiae, Protein Sci. 6, 481-483.
13. Maté, M. J., Zamocky, M., Nykyri, L. M., Herzog, C., Alzari, P. M., Betzel, C., Koller, F., and Fita, I. (1999) Structure of catalase-A from Saccharomyces cerevisiae, J. Mol. Biol. 286, 135-139.
14. Ko, T.-P., Safo, M. K., Musayev, F. N., Di Salvo, M. L., Wang, C., Wu, S.-H., and Abraham, D. J. (1999) Structure of human erythrocyte catalase, Acta Crystallogr. D56, 241-245.
15. Putnam, C. D., Arvai, A. S., Bourne, Y., and Tainer, J. A. (1999) Active and inhibited human catalase structures: Ligand and NADPH binding and catalytic mechanism. J. Mol. Biol. 296, 295-309.
16. Carpena, X., Perez, R., Ochoa, W. F., Verdaguer, N., Klotz, M. G., Switala, J., Melik-Adamyan, W., Fita, I., and Loewen, P. C. (2001) Crystallization and preliminary X-ray analysis of clade I catalases from Pseudomonas syringae and Listeria seeligeri, Acta Crystallogr. D57, 1184-1186.
17. Carpena, X., Soriano, M., Klotz, M. G., Duckworth, H. W., Donald, L. J., Melik-Adamyan, W., Fita, I., and Loewen, P. C. (2003) Structure of the clade I catalase, CatF of Pseudomonas syringae, at 1.8 Å resolution, Proteins 50, 423-436.
18. Loewen, P. C., Carpena, X., Rovira, C., Ivancich, A., Perez-Luque, R., Haas, R., Odenbreit, S., Nicholls, P., and Fita, I. (2004) Structure of Helicobacter pylori catalase, with and without formic acid bound, at 1.6 Å resolution, Biochemistry 43, 3089-3103.
19. Diaz, A., Horjales, E., Rudiño-Piñera, E., Arreola, R., and Hansberg, W. (2004) Unusual Cys-Tyr covalent bond in a large catalase, J. Mol. Biol. 342, 971-985.
20. Håkansson, K. O., Brugna, M., and Tasse, L. (2004) The three-dimensional structure of catalase from Enterococcus faecalis, Acta Crystallogr. D60, 1374-1380.
21. Switala, J., O'Neil, J. O., and Loewen, P. C. (1999) Catalase HPII from Escherichia coli exhibits enhanced resistance to denaturation, Biochemistry 38, 3895-3901.
22. Chelikani, P., Donald, L. J., Duckworth, H. W., and Loewen, P. C. (2003) Hydroperoxidase II of Escherichia coli exhibits enhanced resistance to proteolytic cleavage compared to other catalases, Biochemistry 42, 5729-5735.
23. Loewen, P. C., and Switala, J. (1986) Purification and characterization of catalase HPII from Escherichia coli K12, Biochem. Cell Biol. 64, 638-646.
24. Rørth, M., and Jensen, P. K. (1967) Determination of catalase activity by means of the Clark electrode. Biochim. Biophys. Acta 139, 171-173.
25. Layne, E. (1957) Spectrophotometric and turbidimetric methods for measuring proteins, Methods Enzymol. 3, 447-454.
26. Maté, M. J., Sevinc, M. S., Hu, B., Bujons, J., Bravo, J., Switala, J., Ens, W., Loewen, P. C., and Fita, I. (1999) Mutants that later the covalent structure of catalase hydroperoxidase II from Escherichia coli, J. Biol. Chem. 274, 27717-27725.
27. Collaborative Computational Project, Number 4 (1994) The CCP4 Suite: Programs for Protein Crystallography, Acta Crystallogr. A50, 760-763.
28. Evans, P. R. (1997) Scala, Joint CCP4 and ESF-EACBM Newsletter 33, 22-24.
29. Vagin, A., and Teplyakov, A. (1997) MOLREP: An automated program for molecular replacement, J. Appl. Crystallogr. 30, 1022-1025.
30. Murshudov, G. N., Vagin, A. A., and Dodson, E. J. (1997) Refinement of macromolecular structures by the maximum-likelihood method, Acta Crystallogr. D53, 240-255.
31. Jones, T. A., Zou, J. Y., Cowan, S. W., and Kjeldgaard, M. (1991) Improved methods for building protein models in electron density maps, Acta Crystallogr. A47, 110-119.
32. Kleywegt, G. J., and Jones, T. A. (1994) Detection, delineation, measurement and display of cavities in macromolecule structures, Acta Crystallogr. D50, 178-185.
33. Evans, S. (1993) SETOR: Hardware lighted three-dimensional solid model representations of macromolecules, J. Mol. Graphics 11, 134-138.
34. Kozlovski, V. I., Donald, L. J., Montero-Callado, V., Spicer, V., Loboda, A. V., Chernushevich, I. V., McNabb, J., Ens, W., and Standing, K. G. (2004) Studies of noncovalent complexes of citrate synthase and catalase on a new TOF mass spectrometer with an ESI source, orthogonal injection, and 16 kV acceleration voltage, Desorption 2004, St. Petersburg, Russia, Aug 29-Sept 2.
35. Rostom, A. A., and Robinson, C. V. (1999) Detection of the intact GroEL chaperonin assembly by mass spectrometry, J. Am. Chem. Soc. 121, 4718-4719.
36. Sevinc, M. S., Maté, M. J., Switala, J., Fita, I., and Loewen, P. C. (1999) Role of the lateral channel in catalase HPII of Escherichia coli, Protein Sci. 8, 490-498.
37. Switala, J., and Loewen, P. C. (2002) Diversity of properties among catalases, Arch. Biochem. Biophys. 401, 145-154.
38. Hillar, A., Nicholls, P., Switala, J., and Loewen, P. C. (1994) NADPH binding and control of catalase compound II formation: Comparison of bovine, yeast and Escherichia coli enzymes, Biochem. J. 300, 531-539.
39. Lardinois, O. M., and Rouxhet, P. G. (1994) Characterization of hydrogen peroxide and Superoxide degrading pathways of Aspergillus niger catalase: A steady-state analysis, Free Radical Res. 20, 29-50.
40. Obinger, C., Maj, M., Nicholls, P., and Loewen, P. C. (1997) Activity, peroxide compound formation, and heme d synthesis in Escherichia coli HPII catalase, Arch. Biochem. Biophys. 342, 58-67.
41. Sevinc, M. S., Switala, J., Bravo, J., Fita, I., and Loewen, P. C. (1998) Truncation and heme pocket mutation reduce production of functional catalase HPII in Escherichia coli, Protein Eng. 11, 549-555.
42. Kirkman, H. N., and Gaetani, G. F. (1984) Catalase, a tetrameric enzyme with four tightly bound molecules of NADPH, Proc. Natl. Acad. Sci. U.S.A. 81, 4343-4347.
43. Kirkman, H. N., Galiano, S., and Gaetani, G. (1987) The function of catalase-bound NADPH, J. Biol. Chem. 262, 660-666.
44. Hillar, A., and Nicholls, P. (1992) A mechanism for NADPH inhibition of catalase compound II formation, FEBS Lett. 314, 179-182.
45. Obinger, C., Maj, M., Nicholls, P., and Loewen, P. C. (1997) Activity, peroxide compound formation, and heme d synthesis in Escherichia coli HPII catalase, Arch. Biochem. Biophys. 342, 58-67.