Journal
MOLECULAR CELL
Volume 56, Issue 4, Pages 518-530Publisher
CELL PRESS
DOI: 10.1016/j.molcel.2014.10.005
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Funding
- University of Otago's Division of Health Sciences Career Development postdoctoral fellowships
- ALW grant from the Netherlands Organization for Scientific Research (NWO) [820.02.003]
- JSPS KAKENHI [25440013]
- Netherlands Proteomics Centre
- Grants-in-Aid for Scientific Research [25440013] Funding Source: KAKEN
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CRISPR-Cas is a prokaryotic adaptive immune system that provides sequence-specific defense against foreign nucleic acids. Here we report the structure and function of the effector complex of the Type III-A CRISPR-Cas system of Thermus thermophilus: the Csm complex (TtCsm). TtCsm is composed of five different protein subunits (Csm1-Csm5) with an uneven stoichiometry and a single crRNA of variable size (35-53 nt). The TtCsm crRNA content is similar to the Type III-B Cmr complex, indicating that crRNAs are shared among different subtypes. A negative stain EM structure of the TtCsm complex exhibits the characteristic architecture of Type I and Type III CRISPR-associated ribonucleoprotein complexes. crRNA-protein crosslinking studies show extensive contacts between the Csm3 backbone and the bound crRNA. We show that, like TtCmr, TtCsm cleaves complementary target RNAs at multiple sites. Unlike Type I complexes, interference by TtCsm does not proceed via initial base pairing by a seed sequence.
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