Journal
RNA BIOLOGY
Volume 16, Issue 4, Pages 504-517Publisher
TAYLOR & FRANCIS INC
DOI: 10.1080/15476286.2018.1504546
Keywords
CRISPR; Cas proteins; DNA recognition; PAM; ribonucleoproteins
Categories
Funding
- DFG [FOR1680, RA 2169/1-2]
- International Max-Planck-Research School for Environmental, Cellular, and Molecular Microbiology (IMPRS-Mic)
- Deutsche Forschungsgemeinschaft [FOR1680]
- LOEWE excellence initiative
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Adaptive immunity of prokaryotes is mediated by CRISPR-Cas systems that employ a large variety of Cas protein effectors to identify and destroy foreign genetic material. The different targeting mechanisms of Cas proteins rely on the proper protection of the host genome sequence while allowing for efficient detection of target sequences, termed protospacers. A short DNA sequence, the protospacer-adjacent motif (PAM), is frequently used to mark proper target sites. Cas proteins have evolved a multitude of PAM-interacting domains, which enables them to cope with viral anti-CRISPR measures that alter the sequence or accessibility of PAM elements. In this review, we summarize known PAM recognition strategies for all CRISPR-Cas types. Available structures of target bound Cas protein effector complexes highlight the diversity of mechanisms and domain architectures that are employed to guarantee target specificity.
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