Cited by 538

The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.

The Molecular Architecture for RNA-Guided RNA Cleavage by Cas13a

Liu, Liang, Li, Xueyan, Ma, Jun, Li, Zongqiang, You, Lilan, Wang, Jiuyu, Wang, Min, Zhang, Xinzheng, Wang, Yanli·2017·Cell

Abstract

Cas13a, a type VI-A CRISPR-Cas RNA-guided RNA ribonuclease, degrades invasive RNAs targeted by CRISPR RNA (crRNA) and has potential applications in RNA technology. To understand how Cas13a is activated to cleave RNA, we have determined the crystal structure of Leptotrichia buccalis (Lbu) Cas13a bound to crRNA and its target RNA, as well as the cryo-EM structure of the LbuCas13a-crRNA complex. The crRNA-target RNA duplex binds in a positively charged central channel of the nuclease (NUC) lobe, and Cas13a protein and crRNA undergo a significant conformational change upon target RNA binding. The guide-target RNA duplex formation triggers HEPN1 domain to move toward HEPN2 domain, activating the HEPN catalytic site of Cas13a protein, which subsequently cleaves both single-stranded target and collateral RNAs in a non-specific manner. These findings reveal how Cas13a of type VI CRISPR-Cas systems defend against RNA phages and set the stage for its development as a tool for RNA manipulation.

Overview

Integrity signals

Registry

Crossref · 10.1016/j.cell.2017.06.050

Cites

3 of 3 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Verification

Claims the paper makes

This paper’s full text isn’t openly available, so its claims and self-check weren’t run. The registry and citation checks still apply.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Citations

Cites

Show all 3 references

Research works printed but not linked: 41

  1. Abudayyeh, 2016, C2c2 is a single-component programmable RNA-guided RNA-targeting CRISPR effector, Science, 353, aaf5573, 10.1126/science.aaf5573 · DOI · Paper page
  2. Adams, 2002, PHENIX: building new software for automated crystallographic structure determination, Acta Crystallogr. D Biol. Crystallogr., 58, 1948, 10.1107/S0907444902016657 · DOI · Paper page
  3. Anantharaman, 2013, Comprehensive analysis of the HEPN superfamily: identification of novel roles in intra-genomic conflicts, defense, pathogenesis and RNA processing, Biol. Direct, 8, 15, 10.1186/1745-6150-8-15 · DOI
  4. Anders, 2014, Structural basis of PAM-dependent target DNA recognition by the Cas9 endonuclease, Nature, 513, 569, 10.1038/nature13579 · DOI · Paper page
  5. Barrangou, 2007, CRISPR provides acquired resistance against viruses in prokaryotes, Science, 315, 1709, 10.1126/science.1138140 · DOI · Paper page
  6. Brown, 2015, Tools for macromolecular model building and refinement into electron cryo-microscopy reconstructions, Acta Crystallogr. D Biol. Crystallogr., 71, 136, 10.1107/S1399004714021683 · DOI
  7. East-Seletsky, 2016, Two distinct RNase activities of CRISPR-C2c2 enable guide-RNA processing and RNA detection, Nature, 538, 270, 10.1038/nature19802 · DOI · Paper page
  8. East-Seletsky, 2017, RNA targeting by functionally orthogonal type VI-A CRISPR-Cas enzymes, Mol. Cell, 66, 373, 10.1016/j.molcel.2017.04.008 · DOI · Paper page
  9. Emsley, 2010, Features and development of Coot, Acta Crystallogr. D Biol. Crystallogr., 66, 486, 10.1107/S0907444910007493 · DOI · Paper page
  10. Gorski, 2017, RNA-based recognition and targeting: sowing the seeds of specificity, Nat. Rev. Mol. Cell Biol., 18, 215, 10.1038/nrm.2016.174 · DOI
  11. Hale, 2009, RNA-guided RNA cleavage by a CRISPR RNA-Cas protein complex, Cell, 139, 945, 10.1016/j.cell.2009.07.040 · DOI · Paper page
  12. Han, 2014, Structure of human RNase L reveals the basis for regulated RNA decay in the IFN response, Science, 343, 1244, 10.1126/science.1249845 · DOI
  13. Jiang, 2015, STRUCTURAL BIOLOGY. A Cas9-guide RNA complex preorganized for target DNA recognition, Science, 348, 1477, 10.1126/science.aab1452 · DOI
  14. Jiang, 2016, Structures of a CRISPR-Cas9 R-loop complex primed for DNA cleavage, Science, 351, 867, 10.1126/science.aad8282 · DOI
  15. Kucukelbir, 2014, Quantifying the local resolution of cryo-EM density maps, Nat. Methods, 11, 63, 10.1038/nmeth.2727 · DOI
  16. Lee, 2008, Structure of the dual enzyme Ire1 reveals the basis for catalysis and regulation in nonconventional RNA splicing, Cell, 132, 89, 10.1016/j.cell.2007.10.057 · DOI
  17. Lewis, 2017, Building the class 2 CRISPR-Cas arsenal, Mol. Cell, 65, 377, 10.1016/j.molcel.2017.01.024 · DOI
  18. Li, 2013, Electron counting and beam-induced motion correction enable near-atomic-resolution single-particle cryo-EM, Nat. Methods, 10, 584, 10.1038/nmeth.2472 · DOI
  19. Liu, 2017, Two distant catalytic sites are responsible for C2c2 RNase activities, Cell, 168, 121, 10.1016/j.cell.2016.12.031 · DOI
  20. Makarova, 2015, An updated evolutionary classification of CRISPR-Cas systems, Nat. Rev. Microbiol., 13, 722, 10.1038/nrmicro3569 · DOI · Paper page
  21. Makarova, 2017, SnapShot: Class 1 CRISPR-Cas Systems, Cell, 168, 946, 10.1016/j.cell.2017.02.018 · DOI
  22. Makarova, 2017, SnapShot: Class 2 CRISPR-Cas Systems, Cell, 168, 328, 10.1016/j.cell.2016.12.038 · DOI
  23. Marraffini, 2015, CRISPR-Cas immunity in prokaryotes, Nature, 526, 55, 10.1038/nature15386 · DOI
  24. Mastronarde, 2005, Automated electron microscope tomography using robust prediction of specimen movements, J. Struct. Biol., 152, 36, 10.1016/j.jsb.2005.07.007 · DOI
  25. Mulepati, 2013, In vitro reconstitution of an Escherichia coli RNA-guided immune system reveals unidirectional, ATP-dependent degradation of DNA target, J. Biol. Chem., 288, 22184, 10.1074/jbc.M113.472233 · DOI · Paper page
  26. Niewoehner, 2016, Structural basis for the endoribonuclease activity of the type III-A CRISPR-associated protein Csm6, RNA, 22, 318, 10.1261/rna.054098.115 · DOI
  27. Otwinowski, 1997, Processing of X-Ray diffraction data collected in oscillation mode, Methods Enzymol., 276, 307, 10.1016/S0076-6879(97)76066-X · DOI · Paper page
  28. Pettersen, 2004, UCSF Chimera--a visualization system for exploratory research and analysis, J. Comput. Chem., 25, 1605, 10.1002/jcc.20084 · DOI
  29. Plagens, 2015, DNA and RNA interference mechanisms by CRISPR-Cas surveillance complexes, FEMS Microbiol. Rev., 39, 442, 10.1093/femsre/fuv019 · DOI
  30. Rohou, 2015, CTFFIND4: Fast and accurate defocus estimation from electron micrographs, J. Struct. Biol., 192, 216, 10.1016/j.jsb.2015.08.008 · DOI
  31. Scheres, 2012, RELION: implementation of a Bayesian approach to cryo-EM structure determination, J. Struct. Biol., 180, 519, 10.1016/j.jsb.2012.09.006 · DOI · Paper page
  32. Shmakov, 2015, Discovery and functional characterization of diverse class 2 CRISPR-Cas systems, Mol. Cell, 60, 385, 10.1016/j.molcel.2015.10.008 · DOI · Paper page
  33. Shmakov, 2017, Diversity and evolution of class 2 CRISPR-Cas systems, Nat. Rev. Microbiol., 15, 169, 10.1038/nrmicro.2016.184 · DOI · Paper page
  34. Smargon, 2017, Cas13b is a type VI-B CRISPR-associated RNA-guided RNase differentially regulated by accessory proteins Csx27 and Csx28, Mol. Cell, 65, 618, 10.1016/j.molcel.2016.12.023 · DOI · Paper page
  35. Tang, 2007, EMAN2: an extensible image processing suite for electron microscopy, J. Struct. Biol., 157, 38, 10.1016/j.jsb.2006.05.009 · DOI
  36. van der Oost, 2014, Unravelling the structural and mechanistic basis of CRISPR-Cas systems, Nat. Rev. Microbiol., 12, 479, 10.1038/nrmicro3279 · DOI
  37. Wang, 2008, Structure of an argonaute silencing complex with a seed-containing guide DNA and target RNA duplex, Nature, 456, 921, 10.1038/nature07666 · DOI
  38. Wright, 2016, Biology and applications of CRISPR systems: harnessing nature’s toolbox for genome engineering, Cell, 164, 29, 10.1016/j.cell.2015.12.035 · DOI · Paper page
  39. Yamano, 2016, Crystal structure of Cpf1 in complex with guide RNA and target DNA, Cell, 165, 949, 10.1016/j.cell.2016.04.003 · DOI
  40. Yang, 2016, PAM-dependent target DNA Recognition and cleavage by C2c1 CRISPR-Cas endonuclease, Cell, 167, 1814, 10.1016/j.cell.2016.11.053 · DOI
  41. Zetsche, 2015, Cpf1 is a single RNA-guided endonuclease of a class 2 CRISPR-Cas system, Cell, 163, 759, 10.1016/j.cell.2015.09.038 · DOI · Paper page

Cited by

Sorted by citations

Metadata

Authors
Liu, L., Li, X., Ma, J., Li, Z., You, L., Wang, J., Wang, M., Zhang, X., & Wang, Y.
Venue
Cell
Publisher
Elsevier BV
Published
2017-08
Volume
170
Issue
4
Pages
714-726.e10
ISSN
0092-8674
Cited by
538
References
3
Language
en
Funders
  • Salt Science Research Foundation
  • National Natural Science Foundation of China (31400640, 31570874, 31571335, 91440201)
  • Chinese Academy of Sciences (XDB08010203)
  • Ministry of Science and Technology of the People's Republic of China (2014CB910102)

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review