Cargando…
Histone H3 lysine 56 acetylation by Rtt109 is crucial for chromosome positioning
Correct intranuclear organization of chromosomes is crucial for many genome functions, but the mechanisms that position chromatin are not well understood. We used a layered screen to identify Saccharomyces cerevisiae mutants defective in telomere localization to the nuclear periphery. We find that e...
Autores principales: | Hiraga, Shin-ichiro, Botsios, Sotirios, Donaldson, Anne D. |
---|---|
Formato: | Texto |
Lenguaje: | English |
Publicado: |
The Rockefeller University Press
2008
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2582893/ https://www.ncbi.nlm.nih.gov/pubmed/19001125 http://dx.doi.org/10.1083/jcb.200806065 |
Ejemplares similares
-
Rtt109 slows replication speed by histone N-terminal acetylation
por: Frenkel, Nelly, et al.
Publicado: (2021) -
Structural characterization of the Asf1–Rtt109 interaction and its role in histone acetylation
por: Lercher, Lukas, et al.
Publicado: (2018) -
A Cell-Free Fluorometric High-Throughput Screen for Inhibitors of Rtt109-Catalyzed Histone Acetylation
por: Dahlin, Jayme L., et al.
Publicado: (2013) -
Stoichiometry of Rtt109 complexes with Vps75 and histones H3-H4
por: Akhavantabib, Noushin, et al.
Publicado: (2020) -
Molecular functions of the histone acetyltransferase chaperone complex Rtt109-Vps75
por: Berndsen, Christopher E, et al.
Publicado: (2008)