Active-site clashes prevent the human 3-methyladenine DNA glycosylase from improperly removing bases

Chemistry and Biology

Volumn 9, Issue 9, 2002, Pages 1033-1041

  Connor, Ellen E ^a   Wyatt, Michael D ^a  

^a UNIVERSITY OF SOUTH CAROLINA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

3 METHYLADENINE DEOXYRIBONUCLEIC ACID GLYCOSYLASE; 3-METHYLADENINE-DNA GLYCOSYLASE; ADENINE; DNA BINDING PROTEIN; DNA GLYCOSYLTRANSFERASE; DRUG DERIVATIVE; GLYCOSIDASE; PURINE DERIVATIVE;

ARTICLE; BASE MISPAIRING; BASE PAIRING; BINDING SITE; CHEMISTRY; DNA REPAIR; ENZYME SPECIFICITY; ENZYMOLOGY; GEL MOBILITY SHIFT ASSAY; GENETICS; HUMAN; KINETICS; METABOLISM; PHYSIOLOGY; SACCHAROMYCES CEREVISIAE; SITE DIRECTED MUTAGENESIS;

ADENINE; BASE PAIR MISMATCH; BASE PAIRING; BINDING SITES; DNA GLYCOSYLASES; DNA REPAIR; DNA-BINDING PROTEINS; ELECTROPHORETIC MOBILITY SHIFT ASSAY; HUMANS; KINETICS; MUTAGENESIS, SITE-DIRECTED; N-GLYCOSYL HYDROLASES; PURINES; SACCHAROMYCES CEREVISIAE; SUBSTRATE SPECIFICITY;

SACCHAROMYCES CEREVISIAE;

EID: 0036753352     PISSN: 10745521     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1074-5521(02)00215-6     Document Type: Article

References (42)

1. Hoeijmakers J.H. Genome maintenance mechanisms for preventing cancer. Nature. 411:2001;366-374.
2. Lindahl T., Wood R.D. Quality control by DNA repair. Science. 286:1999;1897-1905.
3. Wood R.D., Mitchell M., Sgouros J., Lindahl T. Human DNA repair genes. Science. 291:2001;1284-1289.
4. Scharer O.D., Jiricny J. Recent progress in the biology, chemistry and structural biology of DNA glycosylases. Bioessays. 23:2001;270-281.
5. McCullough A.K., Dodson M.L., Lloyd R.S. Initiation of base excision repair. glycosylase mechanisms and structures Annu. Rev. Biochem. 68:1999;255-285.
6. Parikh S.S., Mol C.D., Hosfield D.J., Tainer J.A. Envisioning the molecular choreography of DNA base excision repair. Curr. Opin. Struct. Biol. 9:1999;37-47.
7. Wyatt M.D., Allan J.M., Lau A.Y., Ellenberger T.E., Samson L.D. 3-methyladenine DNA glycosylases. structure, function, and biological importance Bioessays. 21:1999;668-676.
8. Singer B., Hang B. What structural features determine repair enzyme specificity and mechanism in chemically modified DNA? Chem. Res. Toxicol. 10:1997;713-732.
9. Saparbaev M., Laval J. Excision of hypoxanthine from DNA containing dIMP residues by the Escherichia coli, yeast, rat, and human alkylpurine DNA glycosylases. Proc. Natl. Acad. Sci. USA. 91:1994;5873-5877.
10. Saparbaev M., Kleibl K., Laval J. Escherichia coli, Saccharomyces cerevisiae, rat and human 3-methyladenine DNA glycosylases repair 1,N6-ethenoadenine when present in DNA. Nucleic Acids Res. 23:1995;3750-3755.
11. Dosanjh M.K., Roy R., Mitra S., Singer B. 1,N6-ethenoadenine is preferred over 3-methyladenine as substrate by a cloned human N-methylpurine-DNA glycosylase (3-methyladenine-DNA glycosylase). Biochemistry. 33:1994;1624-1628.
12. Asaeda A., Ide H., Asagoshi K., Matsuyama S., Tano K., Murakami A., Takamori Y., Kubo K. Substrate specificity of human methylpurine DNA N-glycosylase. Biochemistry. 39:2000;1959-1965.
13. O'Connor T.R. Purification and characterization of human 3-methyladenine-DNA glycosylase. Nucleic Acids Res. 21:1993;5561-5569.
14. Saparbaev M.K., Langouet S., Privezentzev C.V., Guengerich F.P., Cai H., Elder R.H., Laval J. 1,N2-Ethenoguanine, a mutagenic DNA adduct, is a substrate of Escherichia coli mismatch-specific Uracil-DNA glycosylase and human alkylpurine-DNA-N glycosylase. J. Biol. Chem. 277:2002;26987-26993.
15. Abner C.W., Lau A.Y., Ellenberger T., Bloom L.B. Base excision and dna binding activities of human alkyladenine DNA glycosylase are sensitive to the base paired with a lesion. J. Biol. Chem. 276:2001;13379-13387.
16. Saparbaev M., Mani J.C., Laval J. Interactions of the human, rat, Saccharomyces cerevisiae and Escherichia coli 3-methyladenine-DNA glycosylases with DNA containing dIMP residues. Nucleic Acids Res. 28:2000;1332-1339.
17. Wyatt M.D., Samson L.D. Influence of DNA structure on hypoxanthine and 1,N(6)-ethenoadenine removal by murine 3-methyladenine DNA glycosylase. Carcinogenesis. 21:2000;901-908.
18. Lau A., Scharer O., Verdine G., Samson L., Ellenberger T. Crystal structure of a human alkylbase-DNA repair enzyme complexed to DNA. Mechanism for nucleotide flipping and base excision Cell. 95:1998;249-258.
19. Lau A.Y., Wyatt M.D., Glassner B.J., Samson L.D., Ellenberger T. Molecular basis for discriminating between normal and damaged bases by the human alkyladenine glycosylase AAG. Proc. Natl. Acad. Sci. USA. 97:2000;13573-13578.
20. Berdal K.G., Johansen R.F., Seeberg E. Release of normal bases from intact DNA by a native DNA repair enzyme. EMBO J. 17:1998;363-367.
21. Glassner B.J., Rasmussen L.J., Najarian M.T., Posnick L.M., Samson L.D. Generation of a strong mutator phenotype in yeast by imbalanced base excision repair. Proc. Natl. Acad. Sci. USA. 95:1998;9997-10002.
22. Posnick L.M., Samson L.D. Imbalanced base excision repair increases spontaneous mutation and alkylation sensitivity in Escherichia coli. J. Bacteriol. 181:1999;6763-6771.
23. Miao F., Bouziane M., O'Connor T.R. Interaction of the recombinant human methylpurine-DNA glycosylase (MPG protein) with oligodeoxyribonucleotides containing either hypoxanthine or abasic sites. Nucleic Acids Res. 26:1998;4034-4041.
24. Engelward B.P., Allan J.M., Dreslin J.A., Kelly J.D., Gold B., Samson L.D. A chemical and genetic approach together define the biological consequences of 3-methyladenine lesions in the mammalian genome. J. Biol. Chem. 273:1998;5412-5418.
25. Roy R., Biswas T., Hazra T.K., Roy G., Grabowski D.T., Izumi T., Srinivasan G., Mitra S. Specific interaction of wild-type and truncated mouse N-methylpurine-DNA glycosylase with ethenoadenine-containing DNA. Biochemistry. 37:1998;580-589.
26. Scharer O.D., Nash H.M., Jiricny J., Laval J., Verdine G.L. Specific binding of a designed pyrrolidine abasic site analog to multiple DNA glycosylases. J. Biol. Chem. 273:1998;8592-8597.
27. Case-Green S.C., Southern E.M. Studies on the base pairing properties of deoxyinosine by solid phase hybridisation to oligonucleotides. Nucleic Acids Res. 22:1993;131-136.
28. Cruse W.B., Aymani J., Kennard O., Brown T., Jack A.G., Leonard G.A. Refined crystal structure of an octanucleotide duplex with I.T. mismatched base pairs. Nucleic Acids Res. 17:1989;55-72.
29. Xuan J.C., Weber I.T. Crystal structure of a B-DNA dodecamer containing inosine, d(CGCIAATTCGCG), at 2.4 A resolution and its comparison with other B-DNA dodecamers. Nucleic Acids Res. 20:1992;5457-5464.
30. Lindahl T., Sedgwick M., Sekiguchi M., Nakabeppu Y. Regulation and expression of the adaptive response to alkylating agents. Annu. Rev. Biochem. 57:1988;133-157.
31. Hang B., Sagi J., Singer B. Correlation between sequence-dependent glycosylase repair and the thermal stability of oligonucleotide duplexes containing 1,N6 ethenoadenine. J. Biol. Chem. 273:1998;33406-33413.
32. Gallinari P., Jiricny J. A new class of uracil-DNA glycosylases related to human thymine-DNA glycosylase. Nature. 383:1996;735-738.
33. Hendrich B., Hardeland U., Ng H.H., Jiricny J., Bird A. The thymine glycosylase MBD4 can bind to the product of deamination at methylated CpG sites. Nature. 401:1999;301-304.
34. Nilsen H., Krokan H.E. Base excision repair in a network of defence and tolerance. Carcinogenesis. 22:2001;987-998.
35. Kartalou M., Samson L.D., Essigmann J.M. Cisplatin adducts inhibit 1,N(6)-ethenoadenine repair by interacting with the human 3-methyladenine DNA glycosylase. Biochemistry. 39:2000;8032-8038.
36. Biswas T., Clos L.J. 2nd, SantaLucia J. Jr., Mitra S., Roy R. Binding of specific DNA base-pair mismatches by N-methylpurine-DNA glycosylase and its implication in initial damage recognition. J. Mol. Biol. 320:2002;503-513.
37. Vallur A.C., Feller J.A., Abner C.W., Tran R.K., Bloom L.B. Effects of hydrogen bonding within a damaged base pair on the activity of wild-type and DNA-intercalating mutants of human alkyladenine DNA glycosylase. J. Biol. Chem. 277:2002;31673-31678.
38. Kaina B., Fritz G., Ochs K., Haas S., Grombacher T., Dosch J., Christmann M., Lund P., Gregel C.M., Becker K. Transgenic systems in studies on genotoxicity of alkylating agents. critical lesions, thresholds and defense mechanisms Mutat. Res. 405:1998;179-191.
39. Coquerelle T., Dosch J., Kaina B. Overexpression of N-methylpurine-DNA glycosylase in Chinese hamster ovary cells renders them more sensitive to the production of chromosomal aberrations by methylating agents-a case of imbalanced DNA repair. Mutat. Res. 336:1995;9-17.
40. Habraken Y., Laval F. Increased resistance of the Chinese hamster mutant irs1 cells to monofunctional alkylating agents by transfection of the E. coli or mammalian N3-methyladenine-DNA-glycosylase genes. Mutat. Res. 293:1993;187-195.
41. Imperatori L., Damia G., Taverna P., Garattini E., Citti L., Boldrini L., D'Incalci M. 3T3 NIH murine fibroblasts and B78 murine melanoma cells expressing the Escherichia coli N3-methyladenine-DNA glycosylase I do not become resistant to alkylating agents. Carcinogenesis. 15:1994;533-537.
42. Taylor J.D., Ackroyd A.J., Halford S.E. The gel shift assay for the analysis of DNA-protein interactions. Kneale G.C. DNA-Protein Interactions, Vol. 30. 1994;Humana Press, Inc, Totowa, NJ. 263-279.pp.