Structural characterization of the Asf1-Rtt109 interaction and its role in histone acetylation.

Lercher, Lukas; Danilenko, Nataliya; Kirkpatrick, John; Carlomagno, Teresa

dc.contributor.author	Lercher, Lukas
dc.contributor.author	Danilenko, Nataliya
dc.contributor.author	Kirkpatrick, John
dc.contributor.author	Carlomagno, Teresa
dc.date.accessioned	2018-01-18T15:21:31Z
dc.date.available	2018-01-18T15:21:31Z
dc.date.issued	2017-12-29
dc.identifier.citation	Structural characterization of the Asf1-Rtt109 interaction and its role in histone acetylation. 2017 Nucleic Acids Res.	en
dc.identifier.issn	1362-4962
dc.identifier.pmid	29300933
dc.identifier.doi	10.1093/nar/gkx1283
dc.identifier.uri	http://hdl.handle.net/10033/621242
dc.description.abstract	Acetylation of histone H3 at lysine-56 by the histone acetyltransferase Rtt109 in lower eukaryotes is important for maintaining genomic integrity and is required for C. albicans pathogenicity. Rtt109 is activated by association with two different histone chaperones, Vps75 and Asf1, through an unknown mechanism. Here, we reveal that the Rtt109 C-terminus interacts directly with Asf1 and elucidate the structural basis of this interaction. In addition, we find that the H3 N-terminus can interact via the same interface on Asf1, leading to a competition between the two interaction partners. This, together with the recruitment and position of the substrate, provides an explanation of the role of the Rtt109 C-terminus in Asf1-dependent Rtt109 activation.
dc.language.iso	en	en
dc.rights.uri	http://creativecommons.org/licenses/by-nc-sa/4.0/	*
dc.title	Structural characterization of the Asf1-Rtt109 interaction and its role in histone acetylation.	en
dc.type	Article	en
dc.contributor.department	Helmholtz-Zentrum für Infektionsforschung GmbH, Inhoffenstr.7, 38124 Braunschweig, Germany.	en
dc.identifier.journal	Nucleic acids research	en
refterms.dateFOA	2018-06-13T00:07:17Z
html.description.abstract	Acetylation of histone H3 at lysine-56 by the histone acetyltransferase Rtt109 in lower eukaryotes is important for maintaining genomic integrity and is required for C. albicans pathogenicity. Rtt109 is activated by association with two different histone chaperones, Vps75 and Asf1, through an unknown mechanism. Here, we reveal that the Rtt109 C-terminus interacts directly with Asf1 and elucidate the structural basis of this interaction. In addition, we find that the H3 N-terminus can interact via the same interface on Asf1, leading to a competition between the two interaction partners. This, together with the recruitment and position of the substrate, provides an explanation of the role of the Rtt109 C-terminus in Asf1-dependent Rtt109 activation.