Structures of the Cmr-β Complex Reveal the Regulation of the Immunity Mechanism of Type III-B CRISPR-Cas

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Structures of the Cmr-β Complex Reveal the Regulation of the Immunity Mechanism of Type III-B CRISPR-Cas. / Sofos, Nicholas; Feng, Mingxia; Stella, Stefano; Pape, Tillmann; Fuglsang, Anders; Lin, Jinzhong; Huang, Qihong; Li, Yingjun; She, Qunxin; Montoya, Guillermo.

I: Molecular Cell, Bind 79, Nr. 5, 2020, s. 741-757.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Harvard

Sofos, N, Feng, M, Stella, S, Pape, T, Fuglsang, A, Lin, J, Huang, Q, Li, Y, She, Q & Montoya, G 2020, 'Structures of the Cmr-β Complex Reveal the Regulation of the Immunity Mechanism of Type III-B CRISPR-Cas', Molecular Cell, bind 79, nr. 5, s. 741-757. https://doi.org/10.1016/j.molcel.2020.07.008

APA

Sofos, N., Feng, M., Stella, S., Pape, T., Fuglsang, A., Lin, J., Huang, Q., Li, Y., She, Q., & Montoya, G. (2020). Structures of the Cmr-β Complex Reveal the Regulation of the Immunity Mechanism of Type III-B CRISPR-Cas. Molecular Cell, 79(5), 741-757. https://doi.org/10.1016/j.molcel.2020.07.008

Vancouver

Sofos N, Feng M, Stella S, Pape T, Fuglsang A, Lin J o.a. Structures of the Cmr-β Complex Reveal the Regulation of the Immunity Mechanism of Type III-B CRISPR-Cas. Molecular Cell. 2020;79(5):741-757. https://doi.org/10.1016/j.molcel.2020.07.008

Author

Sofos, Nicholas ; Feng, Mingxia ; Stella, Stefano ; Pape, Tillmann ; Fuglsang, Anders ; Lin, Jinzhong ; Huang, Qihong ; Li, Yingjun ; She, Qunxin ; Montoya, Guillermo. / Structures of the Cmr-β Complex Reveal the Regulation of the Immunity Mechanism of Type III-B CRISPR-Cas. I: Molecular Cell. 2020 ; Bind 79, Nr. 5. s. 741-757.

Bibtex

@article{ae90f5a2a78641f7bec2e130bd8ec8c1,
title = "Structures of the Cmr-β Complex Reveal the Regulation of the Immunity Mechanism of Type III-B CRISPR-Cas",
abstract = "Cmr-β is a type III-B CRISPR-Cas complex that, upon target RNA recognition, unleashes a multifaceted immune response against invading genetic elements, including single-stranded DNA (ssDNA) cleavage, cyclic oligoadenylate synthesis, and also a unique UA-specific single-stranded RNA (ssRNA) hydrolysis by the Cmr2 subunit. Here, we present the structure-function relationship of Cmr-β, unveiling how binding of the target RNA regulates the Cmr2 activities. Cryoelectron microscopy (cryo-EM) analysis revealed the unique subunit architecture of Cmr-β and captured the complex in different conformational stages of the immune response, including the non-cognate and cognate target-RNA-bound complexes. The binding of the target RNA induces a conformational change of Cmr2, which together with the complementation between the 5' tag in the CRISPR RNAs (crRNA) and the 3' antitag of the target RNA activate different configurations in a unique loop of the Cmr3 subunit, which acts as an allosteric sensor signaling the self- versus non-self-recognition. These findings highlight the diverse defense strategies of type III complexes.",
author = "Nicholas Sofos and Mingxia Feng and Stefano Stella and Tillmann Pape and Anders Fuglsang and Jinzhong Lin and Qihong Huang and Yingjun Li and Qunxin She and Guillermo Montoya",
note = "Copyright {\textcopyright} 2020 Elsevier Inc. All rights reserved.",
year = "2020",
doi = "10.1016/j.molcel.2020.07.008",
language = "English",
volume = "79",
pages = "741--757",
journal = "Molecular Cell",
issn = "1097-2765",
publisher = "Cell Press",
number = "5",

}

RIS

TY - JOUR

T1 - Structures of the Cmr-β Complex Reveal the Regulation of the Immunity Mechanism of Type III-B CRISPR-Cas

AU - Sofos, Nicholas

AU - Feng, Mingxia

AU - Stella, Stefano

AU - Pape, Tillmann

AU - Fuglsang, Anders

AU - Lin, Jinzhong

AU - Huang, Qihong

AU - Li, Yingjun

AU - She, Qunxin

AU - Montoya, Guillermo

N1 - Copyright © 2020 Elsevier Inc. All rights reserved.

PY - 2020

Y1 - 2020

N2 - Cmr-β is a type III-B CRISPR-Cas complex that, upon target RNA recognition, unleashes a multifaceted immune response against invading genetic elements, including single-stranded DNA (ssDNA) cleavage, cyclic oligoadenylate synthesis, and also a unique UA-specific single-stranded RNA (ssRNA) hydrolysis by the Cmr2 subunit. Here, we present the structure-function relationship of Cmr-β, unveiling how binding of the target RNA regulates the Cmr2 activities. Cryoelectron microscopy (cryo-EM) analysis revealed the unique subunit architecture of Cmr-β and captured the complex in different conformational stages of the immune response, including the non-cognate and cognate target-RNA-bound complexes. The binding of the target RNA induces a conformational change of Cmr2, which together with the complementation between the 5' tag in the CRISPR RNAs (crRNA) and the 3' antitag of the target RNA activate different configurations in a unique loop of the Cmr3 subunit, which acts as an allosteric sensor signaling the self- versus non-self-recognition. These findings highlight the diverse defense strategies of type III complexes.

AB - Cmr-β is a type III-B CRISPR-Cas complex that, upon target RNA recognition, unleashes a multifaceted immune response against invading genetic elements, including single-stranded DNA (ssDNA) cleavage, cyclic oligoadenylate synthesis, and also a unique UA-specific single-stranded RNA (ssRNA) hydrolysis by the Cmr2 subunit. Here, we present the structure-function relationship of Cmr-β, unveiling how binding of the target RNA regulates the Cmr2 activities. Cryoelectron microscopy (cryo-EM) analysis revealed the unique subunit architecture of Cmr-β and captured the complex in different conformational stages of the immune response, including the non-cognate and cognate target-RNA-bound complexes. The binding of the target RNA induces a conformational change of Cmr2, which together with the complementation between the 5' tag in the CRISPR RNAs (crRNA) and the 3' antitag of the target RNA activate different configurations in a unique loop of the Cmr3 subunit, which acts as an allosteric sensor signaling the self- versus non-self-recognition. These findings highlight the diverse defense strategies of type III complexes.

U2 - 10.1016/j.molcel.2020.07.008

DO - 10.1016/j.molcel.2020.07.008

M3 - Journal article

C2 - 32730741

VL - 79

SP - 741

EP - 757

JO - Molecular Cell

JF - Molecular Cell

SN - 1097-2765

IS - 5

ER -

ID: 245618286