Characterization of A Human DNA-Repair Methyltransferase

Clarke, Neil D.

Abstract

Funding Agency

• Agency: National Institute of Health (NIH)
• Institute: National Cancer Institute (NCI)
• Type: First Independent Research Support & Transition (FIRST) Awards (R29)
• Project #: 5R29CA059492-04
• Application #: 2100092
• Study Section: Chemical Pathology Study Section (CPA)
• Project Start: 1993-04-01
• Project End: 1998-03-31
• Budget Start: 1996-04-01
• Budget End: 1997-03-31
• Support Year: 4
• Fiscal Year: 1996

Institution

• Name: Johns Hopkins University
• Department: Internal Medicine/Medicine
• Type: Schools of Medicine
• DUNS #: 045911138
• City: Baltimore
• State: MD
• Country: United States
• Zip Code: 21218

Publications

Brown, L R; Deng, J; Clarke, N D (2000) Dominant sensitization variants of human O(6)-methylguanine-DNA-methyltransferase obtained by a mutational screen of surface residues. Mutat Res 459:81-7

Paalman, S R; Sung, C; Clarke, N D (1997) Specificity of DNA repair methyltransferases determined by competitive inactivation with oligonucleotide substrates: evidence that Escherichia coli Ada repairs O6-methylguanine and O4-methylthymine with similar efficiency. Biochemistry 36:11118-24

Brown, L R; Deng, J; Noll, D M et al. (1997) Construction and overexpression of a synthetic gene for human DNA methylguanine methyltransferase: renaturation and rapid purification of the protein. Protein Expr Purif 9:337-45

Paalman, S R; Noll, D M; Clarke, N D (1997) Formation of a covalent complex between methylguanine methyltransferase and DNA via disulfide bond formation between the active site cysteine and a thiol-containing analog of guanine. Nucleic Acids Res 25:1795-801