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

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...

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Autores principales:	Anuska Das, Travis H. Hand, Chardasia L. Smith, Ethan Wickline, Michael Zawrotny, Hong Li
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2020
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/2cea4907f71b47c69f5853d72886df10
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spelling	oai:doaj.org-article:2cea4907f71b47c69f5853d72886df102021-12-02T10:48:19ZThe molecular basis for recognition of 5′-NNNCC-3′ PAM and its methylation state by Acidothermus cellulolyticus Cas910.1038/s41467-020-20204-12041-1723https://doaj.org/article/2cea4907f71b47c69f5853d72886df102020-12-01T00:00:00Zhttps://doi.org/10.1038/s41467-020-20204-1https://doaj.org/toc/2041-1723Acidothermus 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.Anuska DasTravis H. HandChardasia L. SmithEthan WicklineMichael ZawrotnyHong LiNature PortfolioarticleScienceQENNature Communications, Vol 11, Iss 1, Pp 1-11 (2020)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Anuska Das Travis H. Hand Chardasia L. Smith Ethan Wickline Michael Zawrotny Hong Li The molecular basis for recognition of 5′-NNNCC-3′ PAM and its methylation state by Acidothermus cellulolyticus Cas9
description	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.
format	article
author	Anuska Das Travis H. Hand Chardasia L. Smith Ethan Wickline Michael Zawrotny Hong Li
author_facet	Anuska Das Travis H. Hand Chardasia L. Smith Ethan Wickline Michael Zawrotny Hong Li
author_sort	Anuska Das
title	The molecular basis for recognition of 5′-NNNCC-3′ PAM and its methylation state by Acidothermus cellulolyticus Cas9
title_short	The molecular basis for recognition of 5′-NNNCC-3′ PAM and its methylation state by Acidothermus cellulolyticus Cas9
title_full	The molecular basis for recognition of 5′-NNNCC-3′ PAM and its methylation state by Acidothermus cellulolyticus Cas9
title_fullStr	The molecular basis for recognition of 5′-NNNCC-3′ PAM and its methylation state by Acidothermus cellulolyticus Cas9
title_full_unstemmed	The molecular basis for recognition of 5′-NNNCC-3′ PAM and its methylation state by Acidothermus cellulolyticus Cas9
title_sort	molecular basis for recognition of 5′-nnncc-3′ pam and its methylation state by acidothermus cellulolyticus cas9
publisher	Nature Portfolio
publishDate	2020
url	https://doaj.org/article/2cea4907f71b47c69f5853d72886df10
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The molecular basis for recognition of 5′-NNNCC-3′ PAM and its methylation state by Acidothermus cellulolyticus Cas9

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