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Crystal Structure of the CRISPR-Cas RNA Silencing Cmr Complex Bound to a Target Analog

Osawa, Takuo, Inanaga, Hideko, Sato, Chikara, Numata, Tomoyuki·2015·Molecular Cell
DOI 10.1016/j.molcel.2015.03.018
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  • Type III systems depend on multiprotein Cascade complexes that encompass crRNA, Csm in subtype III-A and Cmr in III-B, although Cas6 is absent in these complexes.

    “Type III systems are similar to Type I in the sense that they also depend on multiprotein Cascade complexes that encompass crRNA, Csm in subtype III-A and Cmr in III-B, although Cas6 is absent in these complexes [47].”

    From CRISPR-Cas: Converting A Bacterial Defence Mechanism into A State-of-the-Art Genetic Manipulation Tool (2019) · cites this paper as [47]

    The Summary identifies a crRNA-containing Cmr complex in type III-B, and Results and Discussion discusses the type III-A Csm complex. In “Evolution of the Type I and III Interference Complexes” (page unavailable), the paper says Cmr resembles Cascade; it does not call type III Csm and Cmr complexes Cascade complexes. Our copy also does not state that Cas6 is absent from those complexes. (LLM, conf=0.88)

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  • This binding enables Cas10-mediated cleavage of the complementary DNA duplex and Cas7-guided cleavage of the ssRNA molecule in intervals of 6 nucleotides.

    “This binding enables Cas10-mediated cleavage of the complementary DNA duplex and Cas7-guided cleavage of the ssRNA molecule in intervals of 6 nucleotides [47,50].”

    From CRISPR-Cas: Converting A Bacterial Defence Mechanism into A State-of-the-Art Genetic Manipulation Tool (2019) · cites this paper as [47]

    The Results and Discussion section explains that target RNA binds the Cmr complex and is cleaved at 6-nucleotide intervals. It identifies Cmr4 as the protein involved in that cleavage and Cas7 as its ortholog in a different complex. The paper studies an ssDNA target analog; it does not support the claim that this binding enables Cas10-mediated cleavage of a complementary DNA duplex. (LLM, conf=0.90)

    Experimental — accuracy not yet measured

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Research works printed but not linked: 50

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Metadata

Authors
Osawa, T., Inanaga, H., Sato, C., & Numata, T.
Venue
Molecular Cell
Publisher
Elsevier BV
Published
2015-05
Volume
58
Issue
3
Pages
418-430
ISSN
1097-2765
DOI
10.1016/j.molcel.2015.03.018
Cited by
138
References
2
Language
en
Licence
Funders
  • Japan Society for the Promotion of Science
  • Ministry of Education, Culture, Sports, Science and Technology
  • Institute for Fermentation, Osaka
  • Kurata Memorial Hitachi Science and Technology Foundation
  • Kato Memorial Bioscience Foundation

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