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TitleMechanism of target site selection by type V-K CRISPR-associated transposases.
Journal, issue, pagesScience, Vol. 382, Issue 6672, Page eadj8543, Year 2023
Publish dateNov 17, 2023
AuthorsJerrin Thomas George / Christopher Acree / Jung-Un Park / Muwen Kong / Tanner Wiegand / Yanis Luca Pignot / Elizabeth H Kellogg / Eric C Greene / Samuel H Sternberg /
PubMed AbstractCRISPR-associated transposases (CASTs) repurpose nuclease-deficient CRISPR effectors to catalyze RNA-guided transposition of large genetic payloads. Type V-K CASTs offer potential technology ...CRISPR-associated transposases (CASTs) repurpose nuclease-deficient CRISPR effectors to catalyze RNA-guided transposition of large genetic payloads. Type V-K CASTs offer potential technology advantages but lack accuracy, and the molecular basis for this drawback has remained elusive. Here, we reveal that type V-K CASTs maintain an RNA-independent, "untargeted" transposition pathway alongside RNA-dependent integration, driven by the local availability of TnsC filaments. Using cryo-electron microscopy, single-molecule experiments, and high-throughput sequencing, we found that a minimal, CRISPR-less transpososome preferentially directs untargeted integration at AT-rich sites, with additional local specificity imparted by TnsB. By exploiting this knowledge, we suppressed untargeted transposition and increased type V-K CAST specificity up to 98.1% in cells without compromising on-target integration efficiency. These findings will inform further engineering of CAST systems for accurate, kilobase-scale genome engineering applications.
External linksScience / PubMed:37972161 / PubMed Central
MethodsEM (single particle)
Resolution8.11 Å
Structure data

EMDB-41280: Non-targeted transpososome from ShCAST
Method: EM (single particle) / Resolution: 8.11 Å

Source
  • [Scytonema hofmanni] UTEX 2349 (bacteria)

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