RTT109/YLL002W Literature Guide Help

Other names published for RTT109: KIM2, REM50, KAT11, YLL002W

RTT109 - Primary Literature (56)

ReferenceOther Genes Addressed
Fillingham J, et al.  (2008) Chaperone control of the activity and specificity of the histone H3 acetyltransferase Rtt109. Mol Cell Biol 28(13):4342-53
Fong CS, et al.  (2008) Oxidant-induced cell-cycle delay in Saccharomyces cerevisiae: the involvement of the SWI6 transcription factor. FEMS Yeast Res 8(3):386-99
Hiraga S, et al.  (2008) Histone H3 lysine 56 acetylation by Rtt109 is crucial for chromosome positioning. J Cell Biol 183(4):641-51
Jessulat M, et al.  (2008) Interacting proteins Rtt109 and Vps75 affect the efficiency of non-homologous end-joining in Saccharomyces cerevisiae. Arch Biochem Biophys 469(2):157-64
Li Q, et al.  (2008) Acetylation of histone H3 lysine 56 regulates replication-coupled nucleosome assembly. Cell 134(2):244-55
Lin C and Yuan YA  (2008) Structural insights into histone h3 lysine 56 acetylation by rtt109. Structure 16(10):1503-10
Miller A, et al.  (2008) Proliferating Cell Nuclear Antigen and ASF1 Modulate Silent Chromatin in Saccharomyces cerevisiae via Lysine 56 on Histone H3. Genetics 179(2):793-809
Park YJ, et al.  (2008) Histone chaperone specificity in Rtt109 activation. Nat Struct Mol Biol 15(9):957-64
Roberts TM, et al.  (2008) Regulation of rtt107 recruitment to stalled DNA replication forks by the cullin rtt101 and the rtt109 acetyltransferase. Mol Biol Cell 19(1):171-80
Stavropoulos P, et al.  (2008) Molecular basis for the autoregulation of the protein acetyl transferase Rtt109. Proc Natl Acad Sci U S A 105(34):12236-41
Tang Y, et al.  (2008) Fungal Rtt109 histone acetyltransferase is an unexpected structural homolog of metazoan p300/CBP. Nat Struct Mol Biol 15(7):738-45
Tang Y, et al.  (2008) Structure of Vps75 and implications for histone chaperone function. Proc Natl Acad Sci U S A 105(34):12206-11
Williams SK, et al.  (2008) Acetylation in the globular core of histone H3 on lysine-56 promotes chromatin disassembly during transcriptional activation. Proc Natl Acad Sci U S A 105(26):9000-9005
Yang B, et al.  (2008) HST3/HST4-dependent deacetylation of lysine 56 of histone H3 in silent chromatin. Mol Biol Cell 19(11):4993-5005
Collins SR, et al.  (2007) Functional dissection of protein complexes involved in yeast chromosome biology using a genetic interaction map. Nature 446(7137):806-10
Curcio MJ, et al.  (2007) S-phase checkpoint pathways stimulate the mobility of the retrovirus-like transposon Ty1. Mol Cell Biol 27(24):8874-85
Driscoll R, et al.  (2007) Yeast Rtt109 promotes genome stability by acetylating histone H3 on lysine 56. Science 315(5812):649-52
Han J, et al.  (2007) Acetylation of Lysine 56 of Histone H3 Catalyzed by RTT109 and Regulated by ASF1 Is Required for Replisome Integrity. J Biol Chem 282(39):28587-96
Han J, et al.  (2007) Rtt109 acetylates histone H3 lysine 56 and functions in DNA replication. Science 315(5812):653-5
Han J, et al.  (2007) The Rtt109-Vps75 Histone Acetyltransferase Complex Acetylates Non-nucleosomal Histone H3. J Biol Chem 282(19):14158-64
Thaminy S, et al.  (2007) Hst3 Is Regulated by Mec1-dependent Proteolysis and Controls the S Phase Checkpoint and Sister Chromatid Cohesion by Deacetylating Histone H3 at Lysine 56. J Biol Chem 282(52):37805-14
Tsubota T, et al.  (2007) Histone H3-K56 acetylation is catalyzed by histone chaperone-dependent complexes. Mol Cell 25(5):703-12
Yuen KW, et al.  (2007) Systematic genome instability screens in yeast and their potential relevance to cancer. Proc Natl Acad Sci U S A 104(10):3925-30
Schneider J, et al.  (2006) Rtt109 is required for proper H3K56 acetylation: a chromatin mark associated with the elongating RNA polymerase II. J Biol Chem 281(49):37270-4
Sundin BA, et al.  (2004) Localization of proteins that are coordinately expressed with Cln2 during the cell cycle. Yeast 21(9):793-800
Scholes DT, et al.  (2001) Multiple regulators of Ty1 transposition in Saccharomyces cerevisiae have conserved roles in genome maintenance. Genetics 159(4):1449-65