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Structural basis for DNase activity of a conserved protein implicated in CRISPR-mediated genome defense.
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- Author(s): Wiedenheft B;Wiedenheft B; Zhou K; Jinek M; Coyle SM; Ma W; Doudna JA
- Source:
Structure (London, England : 1993) [Structure] 2009 Jun 10; Vol. 17 (6), pp. 904-12.
- Publication Type:
Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't
- Language:
English
- Additional Information
- Source:
Publisher: Cell Press Country of Publication: United States NLM ID: 101087697 Publication Model: Print Cited Medium: Internet ISSN: 1878-4186 (Electronic) Linking ISSN: 09692126 NLM ISO Abbreviation: Structure Subsets: MEDLINE
- Publication Information:
Publication: 2000- : Cambridge, Mass. : Cell Press
Original Publication: London : Current Biology, c1993-
- Subject Terms:
- Abstract:
Acquired immunity in prokaryotes is achieved by integrating short fragments of foreign nucleic acids into clustered regularly interspaced short palindromic repeats (CRISPRs). This nucleic acid-based immune system is mediated by a variable cassette of up to 45 protein families that represent distinct immune system subtypes. CRISPR-associated gene 1 (cas1) encodes the only universally conserved protein component of CRISPR immune systems, yet its function is unknown. Here we show that the Cas1 protein is a metal-dependent DNA-specific endonuclease that produces double-stranded DNA fragments of approximately 80 base pairs in length. The 2.2 A crystal structure of the Cas1 protein reveals a distinct fold and a conserved divalent metal ion-binding site. Mutation of metal ion-binding residues, chelation of metal ions, or metal-ion substitution inhibits Cas1-catalyzed DNA degradation. These results provide a foundation for understanding how Cas1 contributes to CRISPR function, perhaps as part of the machinery for processing foreign nucleic acids.
- Comments:
Comment in: Structure. 2009 Jun 10;17(6):786-8. (PMID: 19523896)
- Grant Information:
5R01GM073794-02 United States GM NIGMS NIH HHS; United States Howard Hughes Medical Institute
- Accession Number:
0 (DNA, Bacterial)
0 (Proteins)
EC 3.1.- (Deoxyribonucleases)
- Publication Date:
Date Created: 20090616 Date Completed: 20090924 Latest Revision: 20231127
- Publication Date:
20240829
- Accession Number:
10.1016/j.str.2009.03.019
- Accession Number:
19523907
No Comments.