YNG2/YHR090C Literature Guide Help

Other names published for YNG2: NBN1, EAF4, YHR090C

YNG2 - Primary Literature (24)

ReferenceOther Genes Addressed
Mitchell L, et al.  (2013) mChIP-KAT-MS, a method to map protein interactions and acetylation sites for lysine acetyltransferases. Proc Natl Acad Sci U S A 110(17):E1641-50
Galdieri L and Vancura A  (2012) Acetyl-CoA carboxylase regulates global histone acetylation. J Biol Chem 287(28):23865-76
Arnold KM, et al.  (2011) Processing Mechanism and Substrate Selectivity of the Core NuA4 Histone Acetyltransferase Complex. Biochemistry 50(5):727-37
Chittuluru JR, et al.  (2011) Structure and nucleosome interaction of the yeast NuA4 and Piccolo-NuA4 histone acetyltransferase complexes.LID - 10.1038/nsmb.2128 [doi] Nat Struct Mol Biol ()
Chruscicki A, et al.  (2010) Critical determinants for chromatin binding by Saccharomyces cerevisiae Yng1 exist outside of the plant homeodomain finger. Genetics 185(2):469-77
Hoke SM, et al.  (2010) Mutational analysis of the C-terminal FATC domain of Saccharomyces cerevisiae Tra1. Curr Genet 56(5):447-65
Gordon PM, et al.  (2008) Interspecies data mining to predict novel ING-protein interactions in human. BMC Genomics 9:426
Lin YY, et al.  (2008) A comprehensive synthetic genetic interaction network governing yeast histone acetylation and deacetylation. Genes Dev 22(15):2062-74
Mitchell L, et al.  (2008) Functional dissection of the NuA4 histone acetyltransferase reveals its role as a genetic hub and that Eaf1 is essential for complex integrity. Mol Cell Biol 28(7):2244-56
Berndsen CE, et al.  (2007) Nucleosome recognition by the Piccolo NuA4 histone acetyltransferase complex. Biochemistry 46(8):2091-9
Shi X, et al.  (2007) Proteome-wide Analysis in Saccharomyces cerevisiae Identifies Several PHD Fingers as Novel Direct and Selective Binding Modules of Histone H3 Methylated at Either Lysine 4 or Lysine 36. J Biol Chem 282(4):2450-5
Shi X, et al.  (2006) ING2 PHD domain links histone H3 lysine 4 methylation to active gene repression. Nature 442(7098):96-9
Selleck W, et al.  (2005) The Saccharomyces cerevisiae Piccolo NuA4 histone acetyltransferase complex requires the Enhancer of Polycomb A domain and chromodomain to acetylate nucleosomes. Mol Cell Biol 25(13):5535-42
Utley RT, et al.  (2005) Regulation of NuA4 histone acetyltransferase activity in transcription and DNA repair by phosphorylation of histone H4. Mol Cell Biol 25(18):8179-90
Krogan NJ, et al.  (2004) Regulation of chromosome stability by the histone H2A variant Htz1, the Swr1 chromatin remodeling complex, and the histone acetyltransferase NuA4. Proc Natl Acad Sci U S A 101(37):13513-8
Zhang H, et al.  (2004) The Yaf9 component of the SWR1 and NuA4 complexes is required for proper gene expression, histone H4 acetylation, and Htz1 replacement near telomeres. Mol Cell Biol 24(21):9424-36
Boudreault AA, et al.  (2003) Yeast enhancer of polycomb defines global Esa1-dependent acetylation of chromatin. Genes Dev 17(11):1415-28
Le Masson I, et al.  (2003) Yaf9, a novel NuA4 histone acetyltransferase subunit, is required for the cellular response to spindle stress in yeast. Mol Cell Biol 23(17):6086-102
Nourani A, et al.  (2003) Opposite role of yeast ING family members in p53-dependent transcriptional activation. J Biol Chem 278(21):19171-5
Choy JS and Kron SJ  (2002) NuA4 subunit Yng2 function in intra-S-phase DNA damage response. Mol Cell Biol 22(23):8215-25
Choy JS, et al.  (2001) Yng2p-dependent NuA4 histone H4 acetylation activity is required for mitotic and meiotic progression. J Biol Chem 276(47):43653-62
Nourani A, et al.  (2001) Role of an ING1 growth regulator in transcriptional activation and targeted histone acetylation by the NuA4 complex. Mol Cell Biol 21(22):7629-40
Loewith R, et al.  (2000) Three yeast proteins related to the human candidate tumor suppressor p33(ING1) are associated with histone acetyltransferase activities. Mol Cell Biol 20(11):3807-16
Aasland R, et al.  (1995) The PHD finger: implications for chromatin-mediated transcriptional regulation. Trends Biochem Sci 20(2):56-9