Literature DB >> 25468820

Cutting it close: CRISPR-associated endoribonuclease structure and function.

Megan L Hochstrasser1, Jennifer A Doudna2.   

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.
Copyright © 2014 Elsevier Ltd. All rights reserved.

Entities:  

Keywords:  CRISPR–Cas; Cas5; Cas6; crRNA; endoribonuclease; structure and function

Mesh:

Substances:

Year:  2014        PMID: 25468820     DOI: 10.1016/j.tibs.2014.10.007

Source DB:  PubMed          Journal:  Trends Biochem Sci        ISSN: 0968-0004            Impact factor:   13.807


  51 in total

Review 1.  Structure Principles of CRISPR-Cas Surveillance and Effector Complexes.

Authors:  Tsz Kin Martin Tsui; Hong Li
Journal:  Annu Rev Biophys       Date:  2015-05-27       Impact factor: 12.981

2.  Structural basis of Type IV CRISPR RNA biogenesis by a Cas6 endoribonuclease.

Authors:  Hannah N Taylor; Emily E Warner; Matthew J Armbrust; Valerie M Crowley; Keith J Olsen; Ryan N Jackson
Journal:  RNA Biol       Date:  2019-06-28       Impact factor: 4.652

3.  Grc3 programs the essential endoribonuclease Las1 for specific RNA cleavage.

Authors:  Monica C Pillon; Mack Sobhany; Mario J Borgnia; Jason G Williams; Robin E Stanley
Journal:  Proc Natl Acad Sci U S A       Date:  2017-06-26       Impact factor: 11.205

4.  Fidelity of prespacer capture and processing is governed by the PAM-mediated interactions of Cas1-2 adaptation complex in CRISPR-Cas type I-E system.

Authors:  Kakimani Nagarajan Yoganand; Manasasri Muralidharan; Siddharth Nimkar; Baskaran Anand
Journal:  J Biol Chem       Date:  2019-11-20       Impact factor: 5.157

Review 5.  Cas6 processes tight and relaxed repeat RNA via multiple mechanisms: A hypothesis.

Authors:  Jana Sefcikova; Mitchell Roth; Ge Yu; Hong Li
Journal:  Bioessays       Date:  2017-05-11       Impact factor: 4.345

Review 6.  Casposons: mobile genetic elements that gave rise to the CRISPR-Cas adaptation machinery.

Authors:  Mart Krupovic; Pierre Béguin; Eugene V Koonin
Journal:  Curr Opin Microbiol       Date:  2017-05-01       Impact factor: 7.934

7.  Real-Time Observation of Target Search by the CRISPR Surveillance Complex Cascade.

Authors:  Chaoyou Xue; Yicheng Zhu; Xiangmei Zhang; Yeon-Kyun Shin; Dipali G Sashital
Journal:  Cell Rep       Date:  2017-12-26       Impact factor: 9.423

8.  The history and market impact of CRISPR RNA-guided nucleases.

Authors:  Paul Bg van Erp; Gary Bloomer; Royce Wilkinson; Blake Wiedenheft
Journal:  Curr Opin Virol       Date:  2015-04-26       Impact factor: 7.090

9.  Two distinct RNase activities of CRISPR-C2c2 enable guide-RNA processing and RNA detection.

Authors:  Alexandra East-Seletsky; Mitchell R O'Connell; Spencer C Knight; David Burstein; Jamie H D Cate; Robert Tjian; Jennifer A Doudna
Journal:  Nature       Date:  2016-09-26       Impact factor: 49.962

10.  A Non-Stem-Loop CRISPR RNA Is Processed by Dual Binding Cas6.

Authors:  Yaming Shao; Hagen Richter; Shengfang Sun; Kundan Sharma; Henning Urlaub; Lennart Randau; Hong Li
Journal:  Structure       Date:  2016-03-17       Impact factor: 5.006

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