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Elimination of inter-domain interactions increases the cleavage fidelity of the restriction endonuclease Dralll 被引量:1
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作者 Wei Zhuo Xuhui Lai +5 位作者 Liqing Zhang Siu-Hong Chan Fengjuan Li Zhenyu Zhu Maojun Yang Dapeng Sun 《Protein & Cell》 SCIE CAS CSCD 2014年第5期357-368,共12页
Dralll is a type liP restriction endonucleases (REases) that recognizes and creates a double strand break within the gapped palindromic sequence CACTNNN^GTG of double-stranded DNA indicates nicking on the bottom st... Dralll is a type liP restriction endonucleases (REases) that recognizes and creates a double strand break within the gapped palindromic sequence CACTNNN^GTG of double-stranded DNA indicates nicking on the bottom strand; indicates nicking on the top strand). However, wild type Dralll shows significant star activity. In this study, it was found that the prominent star site is CATSGTT;GTG, consisting of a star 5' half (CAT) and a canonical 3' half (GTG). Dralll nicks the 3' canonical half site at a faster rate than the 5' star half site, in contrast to the similar rate with the canonical full site. The crystal structure of the Dralll protein was solved. It indicated, as supported by mutagenesis, that Dralll possesses a ~13a- metal HNH active site. The structure revealed extensive intra-molecular interactions between the N-terminal domain and the C-terminal domain containing the HNH active site. Disruptions of these interactions through site- directed mutagenesis drastically increased cleavage fidelity. The understanding of fidelity mechanisms will enable generation of high fidelity REases. 展开更多
关键词 dralll restriction endonuclease fidelity substrate specificity star activity inter-domain interactionsite-directed mutagenesis
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