| Title |
Disarming of type I-F CRISPR-Cas surveillance complex by anti-CRISPR proteins AcrIF6 and AcrIF9 |
| Authors |
Kupčinskaitė, Eglė ; Tutkus, Marijonas ; Kopūstas, Aurimas ; Ašmontas, Simonas Vytautas ; Jankunec, Marija ; Zaremba, Mindaugas ; Tamulaitienė, Giedrė ; Šinkūnas, Tomas |
| DOI |
10.1038/s41598-022-19797-y |
| Full Text |
|
| Is Part of |
Scientific reports.. Springer Science and Business Media LLC. 2022, vol. 12, art. no. 15548, p. 1-14.. ISSN 2045-2322. eISSN 2045-2322 |
| Keywords [eng] |
CRISPR-Cas ; anti-CRISPR ; single-molecule level ; fluorescecnce microscopy ; DNA curtains |
| Abstract [eng] |
CRISPR-Cas systems are prokaryotic adaptive immune systems that protect against phages and other invading nucleic acids. The evolutionary arms race between prokaryotes and phages gave rise to phage anti-CRISPR (Acr) proteins that act as a counter defence against CRISPR-Cas systems by inhibiting the effector complex. Here, we used a combination of bulk biochemical experiments, X-ray crystallography and single-molecule techniques to explore the inhibitory activity of AcrIF6 and AcrIF9 proteins against the type I-F CRISPR-Cas system from Aggregatibacter actinomycetemcomitans (Aa). We showed that AcrIF6 and AcrIF9 proteins hinder Aa-Cascade complex binding to target DNA. We solved a crystal structure of Aa1-AcrIF9 protein, which differ from other known AcrIF9 proteins by an additional structurally important loop presumably involved in the interaction with Cascade. We revealed that AcrIF9 association with Aa-Cascade promotes its binding to off-target DNA sites, which facilitates inhibition of CRISPR-Cas protection. |
| Published |
Springer Science and Business Media LLC |
| Type |
Journal article |
| Language |
English |
| Publication date |
2022 |
| CC license |
|
