6opm

Publication Abstract from PubMed

Key to CRISPR-Cas adaptive immunity is maintaining an ongoing record of invading nucleic acids, a process carried out by the Cas1-Cas2 complex that integrates short segments of foreign genetic material (spacers) into the CRISPR locus. It is hypothesized that Cas1 evolved from casposases, a novel class of transposases. We show here that the Methanosarcina mazei casposase can integrate varied forms of the casposon end in vitro, and recapitulates several properties of CRISPR-Cas integrases including site-specificity. The X-ray structure of the casposase bound to DNA representing the product of integration reveals a tetramer with target DNA bound snugly between two dimers in which single-stranded casposon end binding resembles that of spacer 3'-overhangs. The differences between transposase and CRISPR-Cas integrase are largely architectural, and it appears that evolutionary change involved changes in protein-protein interactions to favor Cas2 binding over tetramerization; this in turn led to preferred integration of single spacers over two transposon ends.

Casposase structure and the mechanistic link between DNA transposition and spacer acquisition by CRISPR-Cas.,Hickman AB, Kailasan S, Genzor P, Haase AD, Dyda F Elife. 2020 Jan 8;9. pii: 50004. doi: 10.7554/eLife.50004. PMID:31913120^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.