期刊
SCIENCE
卷 357, 期 6356, 页码 1113-+出版社
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.aao0679
关键词
-
资金
- University of California Office of the President, Multicampus Research Programs and Initiatives grant [MR-15-328599]
- Sandler Foundation
- U.S. Department of Energy (DOE), Office of Science, Office of Basic Energy Sciences [DE-AC02-76SF00515]
- U.S. DOE, Office of Biological and Environmental Research
- National Institutes of Health, National Institute of General Medical Sciences [P41GM103393]
- U.S. National Science Foundation (NSF) grant [1244557]
- National Institute of General Medical Sciences [1P50GM102706-01]
- U.S. NSF Graduate Research Fellowship
- Howard Hughes Medical Institute
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [P01GM051487, P41GM103393, P50GM102706] Funding Source: NIH RePORTER
CRISPR-Cas systems depend on the Cas1-Cas2 integrase to capture and integrate short foreign DNA fragments into the CRISPR locus, enabling adaptation to new viruses. We present crystal structures of Cas1-Cas2 bound to both donor and target DNA in intermediate and product integration complexes, as well as a cryo-electron microscopy structure of the full CRISPR locus integration complex, including the accessory protein IHF (integration host factor). The structures show unexpectedly that indirect sequence recognition dictates integration site selection by favoring deformation of the repeat and the flanking sequences. IHF binding bends the DNA sharply, bringing an upstream recognition motif into contact with Cas1 to increase both the specificity and efficiency of integration. These results explain how the Cas1-Cas2 CRISPR integrase recognizes a sequence-dependent DNA structure to ensure site-selective CRISPR array expansion during the initial step of bacterial adaptive immunity.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据