Structural basis for inhibition of an archaeal CRISPR–Cas type I-D large subunit by an anti-CRISPR protein

Research output: Contribution to journal › Journal article › Research › peer-review

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Structural basis for inhibition of an archaeal CRISPR–Cas type I-D large subunit by an anti-CRISPR protein. / Manav, M. Cemre; Van, Lan B.; Lin, Jinzhong; Fuglsang, Anders; Peng, Xu; Brodersen, Ditlev E.

In: Nature Communications, Vol. 11, 5993, 2020.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Manav, MC, Van, LB, Lin, J, Fuglsang, A, Peng, X & Brodersen, DE 2020, 'Structural basis for inhibition of an archaeal CRISPR–Cas type I-D large subunit by an anti-CRISPR protein', Nature Communications, vol. 11, 5993. https://doi.org/10.1038/s41467-020-19847-x

APA

Manav, M. C., Van, L. B., Lin, J., Fuglsang, A., Peng, X., & Brodersen, D. E. (2020). Structural basis for inhibition of an archaeal CRISPR–Cas type I-D large subunit by an anti-CRISPR protein. Nature Communications, 11, [5993]. https://doi.org/10.1038/s41467-020-19847-x

Vancouver

Manav MC, Van LB, Lin J, Fuglsang A, Peng X, Brodersen DE. Structural basis for inhibition of an archaeal CRISPR–Cas type I-D large subunit by an anti-CRISPR protein. Nature Communications. 2020;11. 5993. https://doi.org/10.1038/s41467-020-19847-x

Author

Manav, M. Cemre ; Van, Lan B. ; Lin, Jinzhong ; Fuglsang, Anders ; Peng, Xu ; Brodersen, Ditlev E. / Structural basis for inhibition of an archaeal CRISPR–Cas type I-D large subunit by an anti-CRISPR protein. In: Nature Communications. 2020 ; Vol. 11.

Bibtex

@article{5ff89966624a48389a645e5731425470,
title = "Structural basis for inhibition of an archaeal CRISPR–Cas type I-D large subunit by an anti-CRISPR protein",
abstract = "A hallmark of type I CRISPR–Cas systems is the presence of Cas3, which contains both the nuclease and helicase activities required for DNA cleavage during interference. In subtype I-D systems, however, the histidine-aspartate (HD) nuclease domain is encoded as part of a Cas10-like large effector complex subunit and the helicase activity in a separate Cas3{\textquoteright} subunit, but the functional and mechanistic consequences of this organisation are not currently understood. Here we show that the Sulfolobus islandicus type I-D Cas10d large subunit exhibits an unusual domain architecture consisting of a Cas3-like HD nuclease domain fused to a degenerate polymerase fold and a C-terminal domain structurally similar to Cas11. Crystal structures of Cas10d both in isolation and bound to S. islandicus rod-shaped virus 3 AcrID1 reveal that the anti-CRISPR protein sequesters the large subunit in a non-functional state unable to form a cleavage-competent effector complex. The architecture of Cas10d suggests that the type I-D effector complex is similar to those found in type III CRISPR–Cas systems and that this feature is specifically exploited by phages for anti-CRISPR defence.",
author = "Manav, {M. Cemre} and Van, {Lan B.} and Jinzhong Lin and Anders Fuglsang and Xu Peng and Brodersen, {Ditlev E.}",
year = "2020",
doi = "10.1038/s41467-020-19847-x",
language = "English",
volume = "11",
journal = "Nature Communications",
issn = "2041-1723",
publisher = "nature publishing group",

}

RIS

TY - JOUR

T1 - Structural basis for inhibition of an archaeal CRISPR–Cas type I-D large subunit by an anti-CRISPR protein

AU - Manav, M. Cemre

AU - Van, Lan B.

AU - Lin, Jinzhong

AU - Fuglsang, Anders

AU - Peng, Xu

AU - Brodersen, Ditlev E.

PY - 2020

Y1 - 2020

N2 - A hallmark of type I CRISPR–Cas systems is the presence of Cas3, which contains both the nuclease and helicase activities required for DNA cleavage during interference. In subtype I-D systems, however, the histidine-aspartate (HD) nuclease domain is encoded as part of a Cas10-like large effector complex subunit and the helicase activity in a separate Cas3’ subunit, but the functional and mechanistic consequences of this organisation are not currently understood. Here we show that the Sulfolobus islandicus type I-D Cas10d large subunit exhibits an unusual domain architecture consisting of a Cas3-like HD nuclease domain fused to a degenerate polymerase fold and a C-terminal domain structurally similar to Cas11. Crystal structures of Cas10d both in isolation and bound to S. islandicus rod-shaped virus 3 AcrID1 reveal that the anti-CRISPR protein sequesters the large subunit in a non-functional state unable to form a cleavage-competent effector complex. The architecture of Cas10d suggests that the type I-D effector complex is similar to those found in type III CRISPR–Cas systems and that this feature is specifically exploited by phages for anti-CRISPR defence.

AB - A hallmark of type I CRISPR–Cas systems is the presence of Cas3, which contains both the nuclease and helicase activities required for DNA cleavage during interference. In subtype I-D systems, however, the histidine-aspartate (HD) nuclease domain is encoded as part of a Cas10-like large effector complex subunit and the helicase activity in a separate Cas3’ subunit, but the functional and mechanistic consequences of this organisation are not currently understood. Here we show that the Sulfolobus islandicus type I-D Cas10d large subunit exhibits an unusual domain architecture consisting of a Cas3-like HD nuclease domain fused to a degenerate polymerase fold and a C-terminal domain structurally similar to Cas11. Crystal structures of Cas10d both in isolation and bound to S. islandicus rod-shaped virus 3 AcrID1 reveal that the anti-CRISPR protein sequesters the large subunit in a non-functional state unable to form a cleavage-competent effector complex. The architecture of Cas10d suggests that the type I-D effector complex is similar to those found in type III CRISPR–Cas systems and that this feature is specifically exploited by phages for anti-CRISPR defence.

U2 - 10.1038/s41467-020-19847-x

DO - 10.1038/s41467-020-19847-x

M3 - Journal article

C2 - 33239638

AN - SCOPUS:85096607677

VL - 11

JO - Nature Communications

JF - Nature Communications

SN - 2041-1723

M1 - 5993

ER -

ID: 253025944