Sequence- and Structure-Specific RNA Processing by a CRISPR Endonuclease
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- 10 September 2010
- journal article
- other
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 329 (5997) , 1355-1358
- https://doi.org/10.1126/science.1192272
Abstract
CRISPR Processing: Many bacteria and archaea recognize invading viruses and plasmids. Foreign DNA is integrated into so-called clustered regularly interspaced short palindromic repeat (CRISPR) loci, and transcripts from these loci are processed into RNAs that can target the invading DNA or RNA for destruction. To investigate the molecular basis for this processing, Haurwitz et al. (p. 1355 ) screened CRISPR-associated (Cas) proteins in the opportunistic pathogen Pseudomonas aeruginosa and found they were capable of cleaving the CRISPR transcripts. The crystal structure of Cas4 with the CRISPR RNA transcript revealed how the protein specifically recognized RNA repeats, as well as the mechanism of endonucleolytic cleavage.Keywords
This publication has 28 references indexed in Scilit:
- CRISPR interference: RNA-directed adaptive immunity in bacteria and archaeaNature Reviews Genetics, 2010
- CRISPR/Cas, the Immune System of Bacteria and ArchaeaScience, 2010
- RNA-Guided RNA Cleavage by a CRISPR RNA-Cas Protein ComplexCell, 2009
- CRISPR Interference Limits Horizontal Gene Transfer in Staphylococci by Targeting DNAScience, 2008
- Cas6 is an endoribonuclease that generates guide RNAs for invader defense in prokaryotesGenes & Development, 2008
- Structural insights into the Cyclin T1–Tat–TAR RNA transcription activation complex from EIAVNature Structural & Molecular Biology, 2008
- Small CRISPR RNAs Guide Antiviral Defense in ProkaryotesScience, 2008
- The CRISPRdb database and tools to display CRISPRs and to generate dictionaries of spacers and repeatsBMC Bioinformatics, 2007
- Evolutionary conservation of sequence and secondary structures in CRISPR repeatsGenome Biology, 2007
- Crystal structure of hypothetical protein TTHB192 from Thermus thermophilus HB8 reveals a new protein family with an RNA recognition motif‐like domainProtein Science, 2006