Protein-mediated folding of the genome is essential for site-specific integration of foreign DNA into CRISPR loci

Author:

Santiago-Frangos Andrew1ORCID,Henriques William1,Wiegand Tanner1ORCID,Gauvin Colin1ORCID,Buyukyoruk Murat1,Neselu Kasahun2,Eng Edward3ORCID,Lander Gabriel4ORCID,Wilkinson Royce1,Graham Ava1,Wiedenheft Blake1ORCID

Affiliation:

1. Montana State University

2. Simons Electron Microscopy Center

3. New York Structural Biology Center

4. Scripps Research

Abstract

Abstract Bacteria and archaea acquire resistance to viruses and plasmids by integrating fragments of foreign DNA into the first repeat of a CRISPR array. However, the mechanism of site-specific integration remains poorly understood. Here, we determine a 560 kDa integration complex structure that explains how Cas (Cas1-2/3) and non-Cas proteins (IHF) fold 150 base-pairs of host DNA into a U-shaped bend and a loop that protrude from Cas1-2/3 at right angles. The U-shaped bend traps foreign DNA on one face of the Cas1-2/3 integrase, while the loop places the first CRISPR repeat in the Cas1 active site. Both Cas3s rotate 100-degrees to expose DNA binding sites on either side of the Cas2 homodimer, that each bind an inverted repeat motif in the leader. Leader sequence motifs direct Cas1-2/3-mediated integration to diverse repeat sequences that have a 5’-GT.

Publisher

Research Square Platform LLC

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4. Fagerlund, R. D. et al. Spacer capture and integration by a type I-F Cas1–Cas2-3 CRISPR adaptation complex. Proc. Natl. Acad. Sci. 114, 201618421 (2017).

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