Journal Article

Crystal structure of NaeI-an evolutionary bridge between DNA endonuclease and topoisomerase

Chen, Yongquan, Topal, Michael D., Luo, Feng, Huai, Qing, Colandene, James D., Ke, Hengming, Zhao, Yingdong

2000

Overview

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 Å 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 λ‐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.

• Publisher: John Wiley & Sons, Ltd,Nature Publishing Group UK,Springer Nature B.V,Oxford University Press
• Subject: Amino Acid Sequence / Amino acids / Bacterial Proteins - chemistry / Binding Sites / CAP / CAP protein / Catalysis / Catalytic Domain / crystal structure / Crystallography / deoxyribonuclease NaeI / Deoxyribonucleases, Type II Site-Specific - chemistry / Deoxyribonucleic acid / DNA / DNA topoisomerase / DNA Topoisomerases, Type I - chemistry / DNA-Binding Proteins - chemistry / Endodeoxyribonucleases - classification / Evolution, Molecular / helix-turn-helix / Models, Molecular / Molecular Sequence Data / NaeI restriction endonuclease / Protein Structure, Quaternary / Synchrotrons