Cutting it close: CRISPR-associated endoribonuclease structure and function. Issue 1 (January 2015)

• Record Type: Journal Article
• Authors: Hochstrasser, Megan L.; Doudna, Jennifer A.
• Is Part Of: Trends in biochemical sciences. Volume 40:Issue 1(2015)
• Page Start: 58
• Page End: 66
• Publication Date: 2015-01
• Subjects: CRISPR–Cas -- crRNA -- Cas5 -- Cas6 -- endoribonuclease -- structure and function; Biochemistry -- Periodicals; 572
• DOI: 10.1016/j.tibs.2014.10.007
• Languages: English
• ISSNs: 0968-0004

Abstract

Highlights: We define the key structural features shared by CRISPR-associated endoRNases. We explain how Cas6 enzymes recognize RNA with high affinity and specificity. We review the cleavage mechanisms of different CRISPR-associated endoribonucleases. We describe the roles of Cas5 and Cas6 proteins in CRISPR interference complexes. We discuss future work and development of Cas6-based biotechnological applications. Abstract : Many bacteria and archaea possess an adaptive immune system consisting of repetitive genetic elements known as clustered regularly interspaced short palindromic repeats (CRISPRs) and CRISPR-associated (Cas) proteins. Similar to RNAi pathways in eukaryotes, CRISPR–Cas systems require small RNAs for sequence-specific detection and degradation of complementary nucleic acids. Cas5 and Cas6 enzymes have evolved to specifically recognize and process CRISPR-derived transcripts into functional small RNAs used as guides by interference complexes. Our detailed understanding of these proteins has led to the development of several useful Cas6-based biotechnological methods. Here, we review the structures, functions, mechanisms, and applications of the enzymes responsible for CRISPR RNA (crRNA) processing, highlighting a fascinating family of endonucleases with exquisite RNA recognition and cleavage activities.