Multisite Substrate Recognition in Asf1-Dependent Acetylation of Histone H3 K56 by Rtt109
Sign Up to like & getrecommendations! Published in 2018 at "Cell"
DOI: 10.1016/j.cell.2018.07.005
Abstract: Rtt109 is a unique histone acetyltransferase acetylating histone H3 lysine 56 (H3K56), a modification critical for DNA replication-coupled nucleosome assembly and genome stability. In cells, histone chaperone Asf1 is essential for H3K56 acetylation, yet the… read more here.
Keywords: acetylation; substrate recognition; histone k56; rtt109 ... See more keywords
Structural basis for the acetylation of histone H3K9 and H3K27 mediated by the histone chaperone Vps75 in Pneumocystis carinii.
Sign Up to like & getrecommendations! Published in 2019 at "Signal transduction and targeted therapy"
DOI: 10.1038/s41392-019-0047-8
Abstract: Rtt109 is a histone acetyltransferase (HAT) that is a potential therapeutic target in conditioned pathogenic fungi Pneumocystis carinii (P. carinii). The histone chaperone Vps75 can stimulate the Rtt109-dependent acetylation of several histone H3 lysines and… read more here.
Keywords: rtt109; acetylation; histone; h3k9 h3k27 ... See more keywords
Structural characterization of the Asf1–Rtt109 interaction and its role in histone acetylation
Sign Up to like & getrecommendations! Published in 2018 at "Nucleic Acids Research"
DOI: 10.1093/nar/gkx1283
Abstract: 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… read more here.
Keywords: acetylation; asf1; role; interaction ... See more keywords
Stoichiometry of Rtt109 complexes with Vps75 and histones H3-H4
Sign Up to like & getrecommendations! Published in 2020 at "Life Science Alliance"
DOI: 10.26508/lsa.202000771
Abstract: The work determines the relative and absolute stoichiometry of a 5-chain protein complex involved in histone chaperoning and acetylation. Using sedimentation velocity and light scattering, it uncovers a dynamic equilibrium of complex self-association. Histone acetylation… read more here.
Keywords: rtt109; vps75 rtt109; stoichiometry rtt109; rtt109 complexes ... See more keywords