ArticleThe Biochemical journal2013
Structure of a dimeric crenarchaeal Cas6 enzyme with an atypical active site for CRISPR RNA processing.
Article in The Biochemical journal, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
24 citing papers in PubMed.
- Archaeal RNA processing and regulation: expanding the functional landscape.Microbiology and molecular biology reviews : MMBR · 2025Review
- A type III-associated Cas6 functions as a negative regulator of type I-B CRISPR-Cas system in Thermus thermophilus.Communications biology · 2025Article
- Article
- Harnessing CRISPR-Cas adaptation for RNA recording and beyond.BMB reports · 2024Review
- Digging into the lesser-known aspects of CRISPR biology.International microbiology : the official journal of the Spanish Society for Microbiology · 2021Review
- CRISPR-Cas adaptive immune systems in Sulfolobales: genetic studies and molecular mechanisms.Science China. Life sciences · 2021Review
- Article
- Origins and evolution of CRISPR-Cas systems.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2019Review
- Article
- Type IV CRISPR RNA processing and effector complex formation in Aromatoleum aromaticum.Nature microbiology · 2019Article
- A Reverse Transcriptase-Cas1 Fusion Protein Contains a Cas6 Domain Required for Both CRISPR RNA Biogenesis and RNA Spacer Acquisition.Molecular cell · 2018Article
- Cas6 processes tight and relaxed repeat RNA via multiple mechanisms: A hypothesis.BioEssays : news and reviews in molecular, cellular and developmental biology · 2017Review
- DNA and RNA interference mechanisms by CRISPR-Cas surveillance complexes.FEMS microbiology reviews · 2015Review
- Biogenesis pathways of RNA guides in archaeal and bacterial CRISPR-Cas adaptive immunity.FEMS microbiology reviews · 2015Review
- CRISPR-Cas Adaptive Immune Systems of the Sulfolobales: Unravelling Their Complexity and Diversity.Life (Basel, Switzerland) · 2015Review
- Structural Principles of CRISPR RNA Processing.Structure (London, England : 1993) · 2015Article
- Annotation and Classification of CRISPR-Cas Systems.Methods in molecular biology (Clifton, N.J.) · 2015Review
- Structure Principles of CRISPR-Cas Surveillance and Effector Complexes.Annual review of biophysics · 2015Review
- An archaeal CRISPR type III-B system exhibiting distinctive RNA targeting features and mediating dual RNA and DNA interference.Nucleic acids research · 2015Article
- Unravelling the structural and mechanistic basis of CRISPR-Cas systems.Nature reviews. Microbiology · 2014Review
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Authors and funding
6 authors.
Funding
Abstract
The competition between viruses and hosts is played out in all branches of life. Many prokaryotes have an adaptive immune system termed 'CRISPR' (clustered regularly interspaced short palindromic repeats) which is based on the capture of short pieces of viral DNA. The captured DNA is integrated into the genomic DNA of the organism flanked by direct repeats, transcribed and processed to generate crRNA (CRISPR RNA) that is loaded into a variety of effector complexes. These complexes carry out sequence-specific detection and destruction of invading mobile genetic elements. In the present paper, we report the structure and activity of a Cas6 (CRISPR-associated 6) enzyme (Sso1437) from Sulfolobus solfataricus responsible for the generation of unit-length crRNA species. The crystal structure reveals an unusual dimeric organization that is important for the enzyme's activity. In addition, the active site lacks the canonical catalytic histidine residue that has been viewed as an essential feature of the Cas6 family. Although several residues contribute towards catalysis, none is absolutely essential. Coupled with the very low catalytic rate constants of the Cas6 family and the plasticity of the active site, this suggests that the crRNA recognition and chaperone-like activities of the Cas6 family should be considered as equal to or even more important than their role as traditional enzymes.
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