Crystal Structure of the Csm1 Subunit of the Csm Complex and Its Single-Stranded DNA-Specific Nuclease Activity

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The CRISPR-Cas system is the RNA-guided immune defense mechanism in bacteria and archaea. Csm1 belongs to the Cas10 family, which is the common signature protein of the type III system. Csm1 is the largest subunit of the Csm interference complex in the type III-A subtype, which targets foreign DNA or RNA. Here, we report crystallographic and biochemical analyses of Thermococcus onnurineus Csm1, revealing a five-domain organization and single-stranded DNA (ssDNA)-specific nuclease activity associated with the N-terminal HD domain. This domain folds into permuted secondary structures in comparison with the HD domain of Cas3 and contains all the catalytically important residues. It exhibited both endo-and exonuclease activities in an Ni2+ or Mn2+-dependent manner. The narrow width of the active-site cleft appears to restrict the substrate specificity to ssDNA and thus to prevent Csm1 from cleaving double-stranded chromosomal DNA. These data suggest that Csm1 may function in DNA interference by the Csm effector complex.
Publisher
CELL PRESS
Issue Date
2015-04
Language
English
Article Type
Article
Keywords

CRISPR-CAS SYSTEMS; GUIDED SURVEILLANCE COMPLEX; SHORT PALINDROMIC REPEATS; RNA SILENCING COMPLEX; IMMUNE-SYSTEM; THERMUS-THERMOPHILUS; INTERFERENCE COMPLEX; ESCHERICHIA-COLI; CASCADE; PROTEIN

Citation

STRUCTURE, v.23, no.4, pp.782 - 790

ISSN
0969-2126
DOI
10.1016/j.str.2015.01.021
URI
http://hdl.handle.net/10203/200756
Appears in Collection
BS-Journal Papers(저널논문)
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