Structural characterization of the Asf1-Rtt109 interaction and its role in histone acetylation.
Cast your vote
You can rate an item by clicking the amount of stars they wish to award to this item.
When enough users have cast their vote on this item, the average rating will also be shown.
Your vote was cast
Thank you for your feedback
Thank you for your feedback
MetadataShow full item record
AbstractAcetylation 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.
CitationStructural characterization of the Asf1-Rtt109 interaction and its role in histone acetylation. 2017 Nucleic Acids Res.
AffiliationHelmholtz-Zentrum für Infektionsforschung GmbH, Inhoffenstr.7, 38124 Braunschweig, Germany.
JournalNucleic acids research
The following license files are associated with this item:
- Creative Commons
Except where otherwise noted, this item's license is described as http://creativecommons.org/licenses/by-nc-sa/4.0/
- Structure of the Rtt109-AcCoA/Vps75 complex and implications for chaperone-mediated histone acetylation.
- Authors: Tang Y, Holbert MA, Delgoshaie N, Wurtele H, Guillemette B, Meeth K, Yuan H, Drogaris P, Lee EH, Durette C, Thibault P, Verreault A, Cole PA, Marmorstein R
- Issue date: 2011 Feb 9
- Two factor authentication: Asf1 mediates crosstalk between H3 K14 and K56 acetylation.
- Authors: Cote JM, Kuo YM, Henry RA, Scherman H, Krzizike DD, Andrews AJ
- Issue date: 2019 Aug 22
- Utilizing targeted mass spectrometry to demonstrate Asf1-dependent increases in residue specificity for Rtt109-Vps75 mediated histone acetylation.
- Authors: Kuo YM, Henry RA, Huang L, Chen X, Stargell LA, Andrews AJ
- Issue date: 2015
- The carboxyl terminus of Rtt109 functions in chaperone control of histone acetylation.
- Authors: Radovani E, Cadorin M, Shams T, El-Rass S, Karsou AR, Kim HS, Kurat CF, Keogh MC, Greenblatt JF, Fillingham JS
- Issue date: 2013 May
- Chaperone-mediated acetylation of histones by Rtt109 identified by quantitative proteomics.
- Authors: Abshiru N, Ippersiel K, Tang Y, Yuan H, Marmorstein R, Verreault A, Thibault P
- Issue date: 2013 Apr 9