The molecular basis for recognition of 5′-NNNCC-3′ PAM and its methylation state by Acidothermus cellulolyticus Cas9

Anuska Das; Travis H. Hand; Chardasia L. Smith; Ethan Wickline; Michael Zawrotny; Hong Li

doi:10.1038/s41467-020-20204-1

Nature Communications (Dec 2020)

The molecular basis for recognition of 5′-NNNCC-3′ PAM and its methylation state by Acidothermus cellulolyticus Cas9

Anuska Das,
Travis H. Hand,
Chardasia L. Smith,
Ethan Wickline,
Michael Zawrotny,
Hong Li

Affiliations

Anuska Das: Institute of Molecular Biophysics, Florida State University
Travis H. Hand: Institute of Molecular Biophysics, Florida State University
Chardasia L. Smith: Institute of Molecular Biophysics, Florida State University
Ethan Wickline: Department of Chemistry and Biochemistry, Florida State University
Michael Zawrotny: Institute of Molecular Biophysics, Florida State University
Hong Li: Institute of Molecular Biophysics, Florida State University

DOI: https://doi.org/10.1038/s41467-020-20204-1
Journal volume & issue: Vol. 11, no. 1
pp. 1 – 11

Abstract

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Acidothermus cellulolyticus CRISPR-Cas9 (AceCas9) is a Type II-C enzyme that cleaves DNA in a Protospacer Adjacent Motif (PAM) methylation sensitive fashion. Biochemical analysis and crystal structures of AceCas9 in complex with sgRNA and DNA bearing the correct and incorrect PAM offer insight into the structural basis for the recognition of PAM and its methylation.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

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