DNA recognition and cleavage by the LAGLIDADG homing endonuclease I-CreI
DNA recognition and cleavage by the LAGLIDADG homing endonuclease I-CreI
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DOI:
10.1016/s1097-2765(00)80146-x
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发表时间:
1998-10-01
期刊:
影响因子:
16
通讯作者:
Stoddard, BL
中科院分区:
文献类型:
--
作者:
Jurica, NS;Monnat, RJ;Stoddard, BL
The structure of the LAGLIDADG intron-encoded homing endonuclease I-Crel bound to homing site DNA has been determined. The interface is formed by an extended, concave beta sheet from each enzyme monomer that contacts each DNA half-site, resulting in direct side-chain contacts to 18 of the 24 base pairs across the full-length homing site. The structure indicates that I-Crel is optimized to its role in genetic transposition by exhibiting long site-recognition while being able to cleave many closely related target sequences. DNA cleavage is mediated by a compact pair of active sites in the I-Crel homodimer, each of which contains a separate bound divalent cation.