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Target RNA activates the protease activity of Craspase to confer antiviral defense.

Liu X, Zhang L, Wang H, Xiu Y, Huang L, Gao Z, Li N, Li F, Xiong W, Gao T, Zhang Y, Yang M, Feng Y
Mol Cell (2022)
Related entries: 7xsp, 7xsq, 7xsr, 7xss, 7xt4

Cited: 11 times
EuropePMC logo PMID: 36306795

Abstract

In the type III-E CRISPR-Cas system, a Cas effector (gRAMP) is associated with a TPR-CHAT to form Craspase (CRISPR-guided caspase). However, both the structural features of gRAMP and the immunity mechanism remain unknown for this system. Here, we report structures of gRAMP-crRNA and gRAMP:cRNA:target RNA as well as structures of Craspase and Craspase complexed with cognate target RNA (CTR) or non-cognate target RNA (NTR). Importantly, the 3' anti-tag region of NTR and CTR binds at two distinct channels in Craspase, and CTR with a non-complementary 3' anti-tag induces a marked conformational change of the TPR-CHAT, which allosterically activates its protease activity to cleave an ancillary protein Csx30. This cleavage then triggers an abortive infection as the antiviral strategy of the type III-E system. Together, our study provides crucial insights into both the catalytic mechanism of the gRAMP and the immunity mechanism of the type III-E system.

Reviews - 7xso mentioned but not cited (1)

  1. Structure and the Mode of Activity of Lon Proteases from Diverse Organisms. Wlodawer A, Sekula B, Gustchina A, Rotanova TV. J Mol Biol 434 167504 (2022)

Articles - 7xso mentioned but not cited (1)

  1. Cryo-EM structure of hexameric yeast Lon protease (PIM1) highlights the importance of conserved structural elements. Yang J, Song AS, Wiseman RL, Lander GC. J Biol Chem 298 101694 (2022)


Reviews citing this publication (1)

  1. Unity among the diverse RNA-guided CRISPR-Cas interference mechanisms. Ganguly C, Rostami S, Long K, Aribam SD, Rajan R. J Biol Chem 300 107295 (2024)

Articles citing this publication (8)

  1. Target RNA-guided protease activity in type III-E CRISPR-Cas system. Wang X, Yu G, Wen Y, An Q, Li X, Liao F, Lian C, Zhang K, Yin H, Wei Y, Deng Z, Zhang H. Nucleic Acids Res 50 12913-12923 (2022)
  2. Structural basis for the non-self RNA-activated protease activity of the type III-E CRISPR nuclease-protease Craspase. Cui N, Zhang JT, Li Z, Liu XY, Wang C, Huang H, Jia N. Nat Commun 13 7549 (2022)
  3. Cryo-EM structure and protease activity of the type III-E CRISPR-Cas effector. Huo Y, Zhao H, Dong Q, Jiang T. Nat Microbiol 8 522-532 (2023)
  4. Letter Craspase: A novel CRISPR/Cas dual gene editor. Huo G, Shepherd J, Pan X. Funct Integr Genomics 23 98 (2023)
  5. An archaeal virus-encoded anti-CRISPR protein inhibits type III-B immunity by inhibiting Cas RNP complex turnover. Liu J, Li Q, Wang X, Liu Z, Ye Q, Liu T, Pan S, Peng N. Nucleic Acids Res 51 11783-11796 (2023)
  6. CRISPR-Cas has a new juggling act: interplay between nuclease and protease. Rish AD, Fu TM. Nat Struct Mol Biol 30 126-128 (2023)
  7. Craspase Orthologs Cleave a Nonconserved Site in Target Protein Csx30. van Beljouw SPB, Haagsma AC, Kalogeropoulos K, Pabst M, Brouns SJJ. ACS Chem Biol 19 1051-1055 (2024)
  8. Structural basis of negative regulation of CRISPR-Cas7-11 by TPR-CHAT. Hong T, Luo Q, Ma H, Wang X, Li X, Shen C, Pang J, Wang Y, Chen Y, Zhang C, Su Z, Dong H, Tang X. Signal Transduct Target Ther 9 111 (2024)


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