+Search query
-Structure paper
Title | TIGR-Tas: A family of modular RNA-guided DNA-targeting systems in prokaryotes and their viruses. |
---|---|
Journal, issue, pages | Science, Vol. 388, Issue 6746, Page eadv9789, Year 2025 |
Publish date | May 1, 2025 |
![]() | Guilhem Faure / Makoto Saito / Max E Wilkinson / Natalia Quinones-Olvera / Peiyu Xu / Daniel Flam-Shepherd / Stephanie Kim / Nishith Reddy / Shiyou Zhu / Lilia Evgeniou / Eugene V Koonin / Rhiannon K Macrae / Feng Zhang / ![]() |
PubMed Abstract | RNA-guided systems provide remarkable versatility, enabling diverse biological functions. Through iterative structural and sequence homology-based mining starting with a guide RNA-interaction domain ...RNA-guided systems provide remarkable versatility, enabling diverse biological functions. Through iterative structural and sequence homology-based mining starting with a guide RNA-interaction domain of Cas9, we identified a family of RNA-guided DNA-targeting proteins in phage and parasitic bacteria. Each system consists of a tandem interspaced guide RNA (TIGR) array and a TIGR-associated (Tas) protein containing a nucleolar protein (Nop) domain, sometimes fused to HNH (TasH)- or RuvC (TasR)-nuclease domains. We show that TIGR arrays are processed into 36-nucleotide RNAs (tigRNAs) that direct sequence-specific DNA binding through a tandem-spacer targeting mechanism. TasR can be reprogrammed for precise DNA cleavage, including in human cells. The structure of TasR reveals striking similarities to box C/D small nucleolar ribonucleoproteins and IS110 RNA-guided transposases, providing insights into the evolution of diverse RNA-guided systems. |
![]() | ![]() ![]() ![]() |
Methods | EM (single particle) |
Resolution | 3.05 Å |
Structure data | EMDB-48616, PDB-9mty: |
Chemicals | ![]() ChemComp-MG: |
Source |
|
![]() | DNA BINDING PROTEIN/RNA/DNA / nuclease / RNA-guided / Nop domain / DNA-binding protein / DNA-RNA HYBRID / DNA BINDING PROTEIN-RNA-DNA complex |