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-Structure paper
Title | RNA targeting by the type III-A CRISPR-Cas Csm complex of Thermus thermophilus. |
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Journal, issue, pages | Mol Cell, Vol. 56, Issue 4, Page 518-530, Year 2014 |
Publish date | Nov 20, 2014 |
Authors | Raymond H J Staals / Yifan Zhu / David W Taylor / Jack E Kornfeld / Kundan Sharma / Arjan Barendregt / Jasper J Koehorst / Marnix Vlot / Nirajan Neupane / Koen Varossieau / Keiko Sakamoto / Takehiro Suzuki / Naoshi Dohmae / Shigeyuki Yokoyama / Peter J Schaap / Henning Urlaub / Albert J R Heck / Eva Nogales / Jennifer A Doudna / Akeo Shinkai / John van der Oost / |
PubMed Abstract | 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 ...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. |
External links | Mol Cell / PubMed:25457165 / PubMed Central |
Methods | EM (single particle) |
Resolution | 17.0 Å |
Structure data | EMDB-6122: |
Source |
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