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Structure paper

TitleMolecular basis for dual-spacer-guided target cleavage by the TIGR-TasH system.
Journal, issue, pagesMol Cell, Vol. 86, Issue 7, Page 1217-11229.e6, Year 2026
Publish dateApr 2, 2026
AuthorsJie Yang / Tongyao Wang / Zhikun Liu / Wenqi Wu / Yangyue Sun / Yancheng Zhan / Shuqin Zhang / Hong Chen / Bin Liu / Caidie Yue / Zhenning Yin / Zhengda Shan / Xuzichao Li / Zhuang Li / Zhiyong Yuan / Hang Yin / Heng Zhang /
PubMed AbstractThe RNA-directed programmable nuclease systems, exemplified by the CRISPR-Cas system, have been widely used in genome editing. In contrast to the single-spacer configuration of CRISPR RNA (crRNA), ...The RNA-directed programmable nuclease systems, exemplified by the CRISPR-Cas system, have been widely used in genome editing. In contrast to the single-spacer configuration of CRISPR RNA (crRNA), the guide RNA (tigRNA) of the tandem interspaced guide RNA (TIGR) system features a dual-spacer arrangement, thereby directing the TIGR-associated (Tas) protein to engage both strands of the target double-stranded DNA (dsDNA). Here, we determine six cryo-electron microscopy structures of the Salicola phage TIGR-TasH complex. The central coiled-coil region of TasH mediates dimerization, while the C-terminal nucleolar protein (Nop) domain is able to autonomously process precursor tigRNA. Upon target binding, the dynamic N-terminal HNH nuclease domain is recruited for cleavage through a β-hairpin, which also determines the target preference. More interestingly, the conserved box C motif of tigRNA stabilizes this β-hairpin in an adenine-specific manner, enabling us to rationally design a guide RNA-defined nickase, distinct from conventional protein-based nickase strategies used in genome editing.
External linksMol Cell / PubMed:41831437
MethodsEM (single particle)
Resolution2.33 - 3.3 Å
Structure data

65487

9vzx

EMDB-65487, PDB-9vzx:
Cryo-EM structure of TasH-tigRNA-gap dsDNA complex
Method: EM (single particle) / Resolution: 2.78 Å

65489

9w02

EMDB-65489, PDB-9w02:
Cryo-EM structure of TasH-tigRNA-ssDNA complex
Method: EM (single particle) / Resolution: 2.72 Å

65490

9w03

EMDB-65490, PDB-9w03:
Cryo-EM structure of TasH-tigRNA complex
Method: EM (single particle) / Resolution: 3.3 Å

65491

9w04

EMDB-65491, PDB-9w04:
Cryo-EM structure of TasH-tigRNA-dsDNA complex
Method: EM (single particle) / Resolution: 2.33 Å

65567

9w26

EMDB-65567, PDB-9w26:
Cryo-EM structure of TasH-tigRNA (5G)-dsDNA complex
Method: EM (single particle) / Resolution: 2.62 Å

67763

21kl

EMDB-67763, PDB-21kl:
Cryo-EM structure of TasH-pre-tigRNA-dsDNA complex
Method: EM (single particle) / Resolution: 3.19 Å

Chemicals

ChemComp-MG:
Unknown entry

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

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