Details
| Originalsprache | Englisch |
|---|---|
| Seiten (von - bis) | 2279-2289 |
| Seitenumfang | 11 |
| Fachzeitschrift | Nucleic acids research |
| Jahrgang | 46 |
| Ausgabenummer | 5 |
| Frühes Online-Datum | 29 Dez. 2017 |
| Publikationsstatus | Veröffentlicht - 16 März 2018 |
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.
ASJC Scopus Sachgebiete
- Biochemie, Genetik und Molekularbiologie (insg.)
- Genetik
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in: Nucleic acids research, Jahrgang 46, Nr. 5, 16.03.2018, S. 2279-2289.
Publikation: Beitrag in Fachzeitschrift › Artikel › Forschung › Peer-Review
}
TY - JOUR
T1 - Structural characterization of the Asf1-Rtt109 interaction and its role in histone acetylation
AU - Lercher, Lukas
AU - Danilenko, Nataliya
AU - Kirkpatrick, John
AU - Carlomagno, Teresa
N1 - Funding Information: L.L. acknowledges the receipt of an EMBO Long-term Fellowship [ALTF 1474-2014, Marie Curie Actions, LTFCO-FUND2013, GA-2103-609409]. Funding for open access charge: University Budget. Conflict of interest statement. None declared.
PY - 2018/3/16
Y1 - 2018/3/16
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=85052659879&partnerID=8YFLogxK
U2 - 10.1093/nar/gkx1283
DO - 10.1093/nar/gkx1283
M3 - Article
C2 - 29300933
AN - SCOPUS:85052659879
VL - 46
SP - 2279
EP - 2289
JO - Nucleic acids research
JF - Nucleic acids research
SN - 0305-1048
IS - 5
ER -