Functional expression of hMYH, a human homolog of the Escherichia coli MutY protein

Journal of Bacteriology

Volumn 181, Issue 19, 1999, Pages 6210-6213

  Slupska, Malgorzata M ^a   Luther, Wendy M ^a   Chiang, Ju Huei ^a   Yang, Hanjing ^a   Miller, Jeffrey H ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

8 HYDROXYDEOXYGUANOSINE; BACTERIAL PROTEIN;

ARTICLE; ENZYME ACTIVITY; ENZYME MECHANISM; ENZYME PURIFICATION; ESCHERICHIA COLI; NONHUMAN; PLASMID; PRIORITY JOURNAL; PROTEIN EXPRESSION; SEQUENCE HOMOLOGY;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; NEGIBACTERIA;

EID: 0032840464     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.181.19.6210-6213.1999     Document Type: Article

References (25)

1. Au, K. G., S. Clark, J. H. Miller, and P. Modrich. 1989. Escherichia coli mutY gene encodes an adenine glycosylase active on G-A mispairs. Proc. Natl. Acad. Sci. USA 86:8877-8881.
2. Cupples, C. G., and J. H. Miller. 1989. A set of lacZ mutations in Escherichia coli that allow rapid detection of each of the six base substitutions. Proc. Natl. Acad. Sci. USA 86:5345-5349.
3. Guan, Y., R. Manuel, A. Arvai, S. Parikh, C. Mol, J. Miller, S. Lloyd, and J. Tainer. 1998. MutY catalytic core, mutant and bound adenine structures define specificity for DNA repair enzyme superfamily. Nat. Struct. Biol. 5: 1058-1064.
4. Krokan, H., R. Standal, and G. Slupphaug. 1997. DNA glycosylases in the base excision repair of DNA. Biochem. J. 325:1-16.
5. Lu, A.-L., and W. P. Fawcett. 1998. Characterization of the recombinant MutY homolog, an adenine DNA glycosylase, from yeast Schizosaccharomyces pombe. J. Biol. Chem. 273:25098-25105.
6. Manuel, R. C., E. W. Czerwinski, and R. S. Lloyd. 1996. Identification of the structural and functional domains of MutY, an Escherichia coli DNA mismatch repair enzyme. J. Biol. Chem. 271:16218-16226.
7. Mattes, R. 1993. Principles of gene expression, p. 233-256. In H.-J. Rehm and G. Reed (ed.), Biotechnology, Vol. II. VCH, Weinheim, Germany.
8. McGoldrick, J. P., Y.-C. Yeh, M. Solomon, J. M. Essigmann, and A.-L. Lu. 1995. Characterization of a mammalian homolog of the Escherichia coli MutY mismatch repair protein. Mol. Cell. Biol. 15:989-996.
9. Miao, F., M. Bouziane, and T. R. O'Connor. 1998. Interaction of the recombinant human methylpurine-DNA glycosylase (MPG protein) with oligodeoxyribonucleotides containing either hypoxanthine or abasic sites. Nucleic Acids Res. 26:4034-4041.
10. Michaels, M. L., C. Cruz, A. P. Grollman, and J. H. Miller. 1992. Evidence that MutY and MutM combine to prevent mutations by an oxidatively damaged form of guanine in DNA. Proc. Natl. Acad. Sci. USA 89:7022-7025.
11. Michaels, M. L., and J. H. Miller. 1992. The GO system protects organisms from the mutagenic effect of the spontaneous lesion 8-hydroxyguanine (7,8-dihydro-8-oxoguanine). J. Bacteriol. 174:6321-6325.
12. Michaels, M. L., L. Pham, Y. Nghiem, C. Cruz, and J. H. Miller. 1990. MutY, an adenine glycosylase active on G-A mispairs, has homology to endonuclease III. Nucleic Acids Res. 18:3841-3845.
13. Michaels, M. L., J. Tchou, A. P. Grollman, and J. H. Miller. 1992. A repair system for 8-oxo-7,8-dihydrodeoxyguanine. Biochemistry 31:10964-10968.
14. Miller, J. H. 1992. A short course in bacterial genetics. A laboratory manual and handbook for Escherichia coli and related bacteria. Cold Spring Harbor Laboratory Press, Plainview, N.Y.
15. Nash, H., S. Bruner, O. Schärer, T. Kawate, T. Addona, E. Spooner, W. Lane, and G. Verdine. 1996. Cloning of a yeast 8-oxoguanine DNA glycosylase reveals the existence of a base-excision DNA-repair protein superfamily. Curr. Biol. 6:968-980.
16. Nghiem, Y., M. Cabrera, C. G. Cupples, and J. H. Miller. 1988. The mutY gene: a mutator locus in Escherichia coli that generates GC→TA transversions. Proc. Natl. Acad. Sci. USA 85:2709-2713.
17. Roy, R., A. Kumar, J. C. Lee, and S. Mitra. 1996. The domains of mammalian base excision repair enzyme N-methylpurine-DNA glycosylase. J. Biol. Chem. 271:23690-23697.
18. ArgtRNAs. BioTechniques 19:196-200.
19. Shibutani, S., M. Takeshita, and A. P. Grollman. 1991. Insertion of specific bases during DNA synthesis past the oxidation-damaged base 8-oxodG. Nature (London) 349:431-434.
20. Slupska, M. M., C. Baikalov, W. M. Luther, J.-H. Chiang, Y.-F. Wei, and J. H. Miller. 1996. Cloning and sequencing a human homolog (hMYH) of the Escherichia coli mutY gene whose function is required for the repair of oxidative DNA damage. J. Bacteriol. 178:3885-3892.
21. Tsai-Wu, J.-J., H.-F. Liu, and A.-L. Lu. 1992. Escherichia coli MutY protein has both N-glycosylase and apurinic/apyrimidinic endonuclease activities on A-C and A-G mispairs. Proc. Natl. Acad. Sci. USA 89:8779-8783.
22. Williams, S. D., and S. S. David. 1998. Evidence that MutY is a monofunctional glycosylase capable of forming a covalent Schiff base intermediate with substrate DNA. Nucleic Acids Res. 26:5123-5133.
23. Yeh, Y.-C., D.-Y. Chang, J. Masin, and A.-L. Lu. 1991. Two nicking enzyme systems specific for mismatch-containing DNA in nuclear extracts from human cells. J. Biol. Chem. 266:6480-6484.
24. Zhang, Q.-M., N. Ishikawa, T. Nakahara, and S. Yonei. 1998. Escherichia coli MutY protein has a guanine-DNA glycosylase that acts on 7,8-dihydro-8-oxoguanine:guanine mispair to prevent spontaneous G:C→C:G transversions. Nucleic Acids Res. 26:4669-4675.
25. Zharkov, D. O., and A. P. Grollman. 1998. MutY DNA glycosylase: base release and intermediate complex formation. Biochemistry 37:12384-12394.