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TitleMolecular basis of single-mismatch-induced nuclease-to-nickase conversion in TIGR-TasH.
Journal, issue, pagesNucleic Acids Res, Vol. 54, Issue 14, Year 2026
Publish dateJul 17, 2026
AuthorsRuimin Zhou / Yancheng Zhan / Yangyue Sun / Runqin Wang / Tongyao Wang / Zhikun Liu / Zhengda Shan / Xuzichao Li / Shuqin Zhang / Nan Sun / Heng Zhang / Zhiyong Yuan / Jie Yang /
PubMed AbstractTandem interspaced guide RNA (TIGR)-Tas systems are a distinct class of RNA-guided double-stranded DNA nucleases that employ dual-spacer guide RNAs (tigRNAs) for PAM-independent target recognition. A ...Tandem interspaced guide RNA (TIGR)-Tas systems are a distinct class of RNA-guided double-stranded DNA nucleases that employ dual-spacer guide RNAs (tigRNAs) for PAM-independent target recognition. A single mismatch between the tigRNA and target DNA can convert Salicola phage CGphi29 (Sp)TasH from a double-strand nuclease into a nickase in a position-dependent manner, but the molecular basis underlying this functional switch remains unknown. Here, we combined biochemical analyses and cryo-electron microscopy to investigate tigRNA maturation and mismatched target recognition by the Nop domain of SpTasH. We show that the Nop domain is required for pre-tigRNA processing and stabilizes the mature tigRNA through extensive interactions, thereby establishing a cleavage-competent ribonucleoprotein complex. Structural analyses of SpTasH complexes bound to substrates containing single mismatches reveal that a mismatch at the 5'-most position of spacer A is readily accommodated through Nop domain-mediated stabilization of the spacer-target heteroduplex. In contrast, a mismatch proximal to the cleavage site destabilizes the heteroduplex, preventing recruitment of the corresponding HNH domain, thereby converting the complex into a nickase. Together, these findings establish the structural basis for position-dependent mismatch recognition and reveal how Nop domain-mediated tigRNA-target stabilization enables differential responses to mismatches, providing a foundation for engineering TIGR-Tas systems for genome-editing applications.
External linksNucleic Acids Res / PubMed:42531075 / PubMed Central
MethodsEM (single particle)
Resolution3.02 - 3.04 Å
Structure data

80301

25qk

EMDB-80301, PDB-25qk:
Cryo-EM structure of TasH-tigRNA-MM1 dsDNA complex
Method: EM (single particle) / Resolution: 3.04 Å

80302

25ql

EMDB-80302, PDB-25ql:
Cryo-EM structure of TasH-tigRNA-MM5 dsDNA complex
Method: EM (single particle) / Resolution: 3.02 Å

Chemicals

ChemComp-MG:
Unknown entry

Source
  • salicola phage cgphi29 (virus)
KeywordsANTIVAL PROTEIN/RNA/DNA / Putative nuclease / ANTIVAL PROTEIN-RNA-DNA complex

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