Mapping the Functional Domains of an Endonuclease

Topal, Michael D.

Abstract

Funding Agency

• Agency: National Institute of Health (NIH)
• Institute: National Institute of General Medical Sciences (NIGMS)
• Type: Research Project (R01)
• Project #: 5R01GM052123-02
• Application #: 2191037
• Study Section: Molecular Biology Study Section (MBY)
• Project Start: 1995-01-01
• Project End: 1998-12-31
• Budget Start: 1996-01-01
• Budget End: 1996-12-31
• Support Year: 2
• Fiscal Year: 1996

Institution

• Name: University of North Carolina Chapel Hill
• Department: Internal Medicine/Medicine
• Type: Schools of Medicine
• DUNS #: 078861598
• City: Chapel Hill
• State: NC
• Country: United States
• Zip Code: 27599

Publications

Carrick, Kevin L; Topal, Michael D (2003) Amino acid substitutions at position 43 of NaeI endonuclease. Evidence for changes in NaeI structure. J Biol Chem 278:9733-9

Colandene, J D; Topal, M D (2000) Evidence for mutations that break communication between the Endo and Topo domains in NaeI endonuclease/topoisomerase. Biochemistry 39:13703-7

Huai, Q; Colandene, J D; Chen, Y et al. (2000) Crystal structure of NaeI-an evolutionary bridge between DNA endonuclease and topoisomerase. EMBO J 19:3110-8

Colandene, J D; Topal, M D (1998) The domain organization of NaeI endonuclease: separation of binding and catalysis. Proc Natl Acad Sci U S A 95:3531-6

Jo, K; Topal, M D (1998) Step-wise DNA relaxation and decatenation by NaeI-43K. Nucleic Acids Res 26:2380-4

Jo, K; Topal, M D (1996) Effects on NaeI-DNA recognition of the leucine to lysine substitution that transforms restriction endonuclease NaeI to a topoisomerase: a model for restriction endonuclease evolution. Nucleic Acids Res 24:4171-5

Jo, K; Topal, M D (1996) Changing a leucine to a lysine residue makes NaeI endonuclease hypersensitive to DNA intercalative drugs. Biochemistry 35:10014-8