Mutational, NMR, and NH Exchange Studies of the Tight and Selective Binding of 8-Oxo-dGMP by the MutT Pyrophosphohydrolase

Biochemistry

Volumn 43, Issue 12, 2004, Pages 3404-3414

  Saraswat, Vibhor ^a   Azurmendi, Hugo F ^a   Mildvan, Albert S ^a  

^a JOHNS HOPKINS UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BINDING ENERGY; ENZYME INHIBITION; ENZYMES; HYDROGEN BONDS; MUTAGENESIS; NUCLEAR MAGNETIC RESONANCE; SOLUTIONS; TERNARY SYSTEMS;

MUTATIONS; PRODUCT INHIBITION;

BIOCHEMISTRY;

8 HYDROXYDEOXYGUANOSINE PHOSPHATE; DEOXYGUANOSINE PHOSPHATE; DEOXYGUANOSINE TRIPHOSPHATE; HYDROGEN; INORGANIC PYROPHOSPHATASE; NUCLEOTIDE; PROTEIN MUTT; PURINE DERIVATIVE; UNCLASSIFIED DRUG;

ARTICLE; BINDING AFFINITY; BINDING SITE; COMPLEX FORMATION; CONFORMATIONAL TRANSITION; ENZYME ACTIVE SITE; ENZYME CONFORMATION; ENZYME STRUCTURE; HYDROGEN BOND; MUTAGENESIS; MUTATIONAL ANALYSIS; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN TERTIARY STRUCTURE; PROTON NUCLEAR MAGNETIC RESONANCE;

5'-GUANYLIC ACID; ALANINE; ARGININE; ASPARAGINE; BINDING SITES; DEUTERIUM EXCHANGE MEASUREMENT; DNA MUTATIONAL ANALYSIS; ESCHERICHIA COLI PROTEINS; HYDROGEN BONDING; KINETICS; LIGANDS; MAGNESIUM; MUTAGENESIS, SITE-DIRECTED; NITROGEN ISOTOPES; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PHOSPHORIC MONOESTER HYDROLASES; PROTEIN BINDING; PROTONS; PYROPHOSPHATASES; THERMODYNAMICS;

EID: 1642284796     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi030216o     Document Type: Article

References (30)

1. Mildvan, A. S., Weber, D. J., and Abeygunawardana, C. (1999) Solution structure and mechanism of the MutT pyrophosphohydrolase, Adv. Enzymol. Relat. Areas Mol. Biol. 73, 183-207.
2. Abeygunawardana, C., Weber, D. J., Gittis, A. G., Frick, D. N., Lin, J., Miller, A.-F., Bessman, M. J., and Mildvan, A. S. (1995) Solution structure of the MutT enzyme, a nucleoside triphosphate pyrophosphohydrolase, Biochemistry 34, 14997-15005.
3. 2+ complex and mechanism of its pyrophosphohydrolase action, Biochemistry 36, 1199-1211.
4. Saraswat, V., Massiah, M. A., Lopez, G., Amzel, L. M., and Mildvan, A. S. (2002) Interactions of the products 8-oxo-dGMP, dGMP, and pyrophosphate with the MutT nucleoside triphosphate pyrophosphohydrolase, Biochemistry 41, 15566-15577.
5. Harris, T. K., Wu, G., Massiah, M. A., and Mildvan, A. S. (2000) Mutational, kinetic, and NMR studies of the roles of conserved glutamate residues and of Lys-39 in the mechanism of the MutT pyrophosphohydrolase, Biochemistry 39, 1655-1674.
6. Bessman, M. J., Frick, D. N., and O'Handley, S. F. (1996) The MutT proteins or "nudix" hydrolases, a family of versatile, widely distributed "housecleaning" enzymes, J. Biol. Chem. 271, 25059-25062.
7. Maki, H., and Sekiguchi, M. (1992) MutT protein specifically hydrolyzes a potent mutagenic substrate for DNA synthesis, Nature 355, 273-275.
8. Shibutani, S., Takeshita, M., and Grollman, A. P. (1991) Insertion of specific bases during DNA synthesis past the oxidation damaged base 8-oxodG, Nature 349, 431-434.
9. Cheng, K. C., Cahill, D. S., Kasai, H., Nishimura, S., and Loeb, L. A. (1992) 8-Hydroxyguanine, an abundant form of oxidative DNA damage causes G→T and A→C substitutions, J. Biol. Chem. 267, 166-172.
10. Treffers, H. P., Spinelli, V., and Belser, N. O. (1954) A new factor (or mutator gene) influencing mutation rates in Escherichia coli, Proc. Natl. Acad. Sci. U.S.A. 40, 1064-1071.
11. Yanofsky, C., Cox, E. C., and Horn, V. (1966) The unusual mutagenic specificity of an E. coli mutator gene, Proc. Natl. Acad. Sci. U.S.A. 55, 274-281.
12. Tsuzuki, T., Egashira, A., Igarashi, H., Iwakuma, T., Nakatsuru, Y., Tominaga, Y., Kawate, H., Nakao, K., Nakamura, K., Ide, F., Kura, S., Nakabeppu, Y., Katsuki, M., Ishikawa, T., and Sekiguchi, M. (2001) Spontaneous tumorigenesis in mice defective in the MTH1 gene encoding 8-oxo-dGTPase, Proc. Natl. Acad. Sci. U.S.A. 98, 11456-11461.
13. Tassotto, M. L., and Mathews, C. K. (2002) Assessing the metabolic function of the MutT 8-oxo-dGTPase in Escherichia coli by nucleotide pool analysis, J. Biol. Chem. 277, 15807-15812.
14. 2+ and 8-oxo-dGMP, a tightly bound product, Biochemistry 42, 10140-10154.
15. Frick, D. N., Weber, D. J., Abeygunawardana, C., Gittis, A. G., Bessman, M. J., and Mildvan, A. S. (1995) NMR studies of the conformations and location of nucleotides bound to the Escherichia coli MutT enzyme, Biochemistry 34, 5577-5586.
16. 2+-8-oxo-dGMP complex, Biochemistry 42, 8616.
17. 15N resonances of the MutT enzyme by heteronuclear multidimensional NMR, Biochemistry 32, 13071-13080.
18. Frick, D. N., Weber, D. J., Gillespie, J. R., Bessman, M. J., and Mildvan, A. S. (1994) Dual divalent cation requirement of the MutT dGTPase, J. Biol. Chem. 269, 1794-1803.
19. Dawson, R. M. C., Eliot, D. C., Eliot, W. H., and Jones, K. M. (1986) Data for Biochemical Research, p 105, Oxford University Press, New York.
20. Trilink Biotechnologies, Inc. (1999) San Diego (product data sheet).
21. Kay, L. E., Keifer, P., and Saarinen, T. (1992) Pure absorption gradient enhanced heteronuclear single quantum coherence spectroscopy with improved sensitivity, J. Am. Chem. Soc. 114, 10663-10665.
22. Delaglio, F., Grzesiek, S., Vuister, G. W., Zhu, G., Pfeifer, J., and Bax, A. (1995) A multidimensional spectral processing system based on Unix Pipes, J. Biomol. NMR 6, 277-293.
23. Goddard, T. D., and Kneller, D. G. (2002) SPARKY 3, University of California, San Francisco.
24. Bai, Y., Milne, J. S., Mayne, L., and Englander, S. W. (1993) Protein stability parameters measured by hydrogen exchange, Proteins: Struct., Funct., Genet. 17, 75-86.
25. Rebholz, K. L., and Northrop, D. B. (1995) Kinetics of iso mechanisms, Methods Enzymol. 249, 211-240.
26. Mildvan, A. S., Weber, D. J., and Kuliopulos, A. (1992) Quantitative interpretations of double mutations of enzymes, Arch. Biochem. Biophys. 294, 327-340.
27. Sakai, Y., Furuichi, M., Takahashi, M., Mishima, M., Iwai, S., Shirakawa, M., and Nakabeppu, Y. (2002) A molecular basis for the selective recognition of 2-hydroxydATP and 8-oxo-dGTP by human MTH1, J. Biol. Chem. 277, 8579-8587.
28. Bruner, S. D., Norman, D. P. G., and Verdine, G. L. (2000) Structural basis for recognition and repair of the endogenous mutagen 8-oxoguanine in DNA, Nature 403, 859-866.
29. Fromme, J. C., and Verdine, G. L. (2002) Structural insights into lesion recognition and repair by the bacterial 8-oxoguanine DNA glycosylase, Nat. Struct. Biol. 9, 544-552.
30. Mahuren, J. D., Coburn, S. P., Slominski, A., and Wortsman, J. (2001) Microassay of phosphate provides a general method for measuring the activity of phosphatases using physiological, nonchromogenic substrates such as lysophosphatidic acid, Anal. Biochem. 298, 241-245.