| Structural highlights
Function
[ASF1_YEAST] Histone chaperone that facilitates histone deposition and histone exchange and removal during nucleosome assembly and disassembly. Facilitates histone deposition through both replication-dependent and replication-independent chromatin assembly pathways. Cooperates with chromatin assembly factor 1 (CAF-1) to promote replication-dependent chromatin assembly and with the HIR complex to promote replication-independent chromatin assembly, which may occur during transcription and DNA repair. May be required for the maintenance of a subset of replication elongation factors, including DNA polymerase epsilon, the RFC complex and PCNA, at stalled replication forks. Also required for acetylation of histone H3 on 'Lys-9' and 'Lys-56'.[1] [2] [3] [4] [5] [6] [7] [8] [9] [10] [11] [12] [13] [14] [15] [16] [17] [18] [19] [20] [21] [22] [23] [24] [25] [26] [27] [28] [29] [30] [31] [32] [33] [34] [35] [36] [37] [38] [39]
Publication Abstract from PubMed
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.
Structural characterization of the Asf1-Rtt109 interaction and its role in histone acetylation.,Lercher L, Danilenko N, Kirkpatrick J, Carlomagno T Nucleic Acids Res. 2017 Dec 29. pii: 4781507. doi: 10.1093/nar/gkx1283. PMID:29300933[40]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
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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. Nucleic Acids Res. 2017 Dec 29. pii: 4781507. doi: 10.1093/nar/gkx1283. PMID:29300933 doi:http://dx.doi.org/10.1093/nar/gkx1283
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