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

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Lercher, L.; Danilenko, N.; Kirkpatrick, J.; Carlomagno, T.: Structural characterization of the Asf1-Rtt109 interaction and its role in histone acetylation. In: Nucleic Acids Research 46 (2018), Nr. 5, S. 2279-2289. DOI: https://doi.org/10.1093/nar/gkx1283

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To cite the version in the repository, please use this identifier: https://doi.org/10.15488/4170

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Sum total of downloads: 93




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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.
License of this version: CC BY-NC 4.0 Unported
Document Type: Article
Publishing status: publishedVersion
Issue Date: 2018
Appears in Collections:Naturwissenschaftliche Fakultät

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pos. country downloads
total perc.
1 image of flag of Germany Germany 50 53.76%
2 image of flag of United States United States 19 20.43%
3 image of flag of Russian Federation Russian Federation 5 5.38%
4 image of flag of China China 5 5.38%
5 image of flag of Indonesia Indonesia 4 4.30%
6 image of flag of Czech Republic Czech Republic 4 4.30%
7 image of flag of United Kingdom United Kingdom 2 2.15%
8 image of flag of Japan Japan 1 1.08%
9 image of flag of Italy Italy 1 1.08%
10 image of flag of France France 1 1.08%
    other countries 1 1.08%

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