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- Title
Crystal structure of NaeI-an evolutionary bridge between DNA endonuclease and topoisomerase.
- Authors
Huai, Q; Colandene, J D; Chen, Y; Luo, F; Zhao, Y; Topal, M D; Ke, H
- Abstract
NAE:I is transformed from DNA endonuclease to DNA topoisomerase and recombinase by a single amino acid substitution. The crystal structure of NAE:I was solved at 2.3 A resolution and shows that NAE:I is a dimeric molecule with two domains per monomer. Each domain contains one potential DNA recognition motif corresponding to either endonuclease or topoisomerase activity. The N-terminal domain core folds like the other type II restriction endonucleases as well as lambda-exonuclease and the DNA repair enzymes MutH and Vsr, implying a common evolutionary origin and catalytic mechanism. The C-terminal domain contains a catabolite activator protein (CAP) motif present in many DNA-binding proteins, including the type IA and type II topoisomerases. Thus, the NAE:I structure implies that DNA processing enzymes evolved from a few common ancestors. NAE:I may be an evolutionary bridge between endonuclease and DNA processing enzymes.
- Publication
The EMBO journal, 2000, Vol 19, Issue 12, p3110
- ISSN
0261-4189
- Publication type
Journal Article
- DOI
10.1093/emboj/19.12.3110