期刊
STRUCTURE
卷 19, 期 2, 页码 257-264出版社
CELL PRESS
DOI: 10.1016/j.str.2010.11.014
关键词
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资金
- NSF [0817638]
- NIH [R01 GM54682]
- U. S. Department of Energy, Office of a Science, Office of Basic Energy Sciences [W-31-109-Eng-38]
- Direct For Biological Sciences
- Div Of Molecular and Cellular Bioscience [0817638] Funding Source: National Science Foundation
The CRISPRs (Clustered Regularly Interspaced Short Palindromic Repeats) found in prokaryotic genomes confer small RNA-mediated protection against viruses and other invaders. CRISPR loci contain iterations of a short repeat sequence alternating with small segments of varying invader-derived sequences. Distinct families of CRISPR-associated Cas proteins function to cleave within the repeat sequence of CRISPR transcripts and produce the individual invader-targeting crRNAs. Here, we report the crystal structure of Pyrococcus furiosus Cas6 bound with a repeat RNA at 3.2 angstrom resolution. In contrast to other Cas families of endonucleases, Cas6 clasps nucleotides 2-9 of the repeat RNA using its two ferredoxin-like domains, and the enzyme-anchored 5' end tethers the distal cleavage site of the RNA between nucleotides 22 and 23 to the predicted enzyme active site on the opposite side of the ferrodoxin-like domains. Our findings suggest a wrap-around mechanism for CRISPR RNA recognition and cleavage by Cas6 and related processing endonucleases.
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