HST2/YPL015C Literature Guide Help

Other names published for HST2: YPL015C

HST2 - Function/Process (25)

ReferenceOther Genes Addressed
Bheda P, et al.  (2012) Biotinylation of lysine method identifies acetylated histone H3 lysine 79 in Saccharomyces cerevisiae as a substrate for Sir2. Proc Natl Acad Sci U S A 109(16):E916-25
Orozco H, et al.  (2012) Wine yeast sirtuins and Gcn5p control aging and metabolism in a natural growth medium. Mech Ageing Dev 133(5):348-358
Tung SY, et al.  (2012) Chromatin affinity-precipitation using a small metabolic molecule: its application to analysis of O-acetyl-ADP-ribose. Cell Mol Life Sci 69(4):641-50
Sanders BD, et al.  (2009) Identification and characterization of novel sirtuin inhibitor scaffolds. Bioorg Med Chem 17(19):7031-41
Lee S, et al.  (2008) Quantification of endogenous sirtuin metabolite O-acetyl-ADP-ribose. Anal Biochem 383(2):174-9
Kaeberlein M, et al.  (2006) Comment on "HST2 mediates SIR2-independent life-span extension by calorie restriction". Science 312(5778):1312; author reply 1312
Khan AN and Lewis PN  (2006) Use of substrate analogs and mutagenesis to study substrate binding and catalysis in the Sir2 family of NAD-dependent protein deacetylases. J Biol Chem 281(17):11702-11
Vaquero A, et al.  (2006) SirT2 is a histone deacetylase with preference for histone H4 Lys 16 during mitosis. Genes Dev 20(10):1256-61
Khan AN and Lewis PN  (2005) Unstructured Conformations Are a Substrate Requirement for the Sir2 Family of NAD-dependent Protein Deacetylases. J Biol Chem 280(43):36073-8
Lamming DW, et al.  (2005) HST2 mediates SIR2-independent life-span extension by calorie restriction. Science 309(5742):1861-4
Borra MT, et al.  (2004) Substrate specificity and kinetic mechanism of the Sir2 family of NAD+-dependent histone/protein deacetylases. Biochemistry 43(30):9877-87
Halme A, et al.  (2004) Genetic and epigenetic regulation of the FLO gene family generates cell-surface variation in yeast. Cell 116(3):405-15
Jacobson SJ, et al.  (2004) Functional analyses of chromatin modifications in yeast. Methods Enzymol 377:3-55
Posakony J, et al.  (2004) Identification and characterization of Sir2 inhibitors through phenotypic assays in yeast. Comb Chem High Throughput Screen 7(7):661-8
Zhao K, et al.  (2004) Structural basis for nicotinamide cleavage and ADP-ribose transfer by NAD(+)-dependent Sir2 histone/protein deacetylases. Proc Natl Acad Sci U S A 101(23):8563-8
Bedalov A, et al.  (2003) NAD+-dependent deacetylase Hst1p controls biosynthesis and cellular NAD+ levels in Saccharomyces cerevisiae. Mol Cell Biol 23(19):7044-54
North BJ, et al.  (2003) The human Sir2 ortholog, SIRT2, is an NAD+-dependent tubulin deacetylase. Mol Cell 11(2):437-44
Starai VJ, et al.  (2003) Short-chain fatty acid activation by acyl-coenzyme A synthetases requires SIR2 protein function in Salmonella enterica and Saccharomyces cerevisiae. Genetics 163(2):545-55
Zhao K, et al.  (2003) Structure and autoregulation of the yeast Hst2 homolog of Sir2. Nat Struct Biol 10(10):864-71
Zhao K, et al.  (2003) Structure of the yeast Hst2 protein deacetylase in ternary complex with 2'-O-acetyl ADP ribose and histone peptide. Structure 11(11):1403-11
Perrod S, et al.  (2001) A cytosolic NAD-dependent deacetylase, Hst2p, can modulate nucleolar and telomeric silencing in yeast. EMBO J 20(1-2):197-209
Landry J, et al.  (2000) The silencing protein SIR2 and its homologs are NAD-dependent protein deacetylases. Proc Natl Acad Sci U S A 97(11):5807-11
Smith JS, et al.  (2000) A phylogenetically conserved NAD+-dependent protein deacetylase activity in the Sir2 protein family. Proc Natl Acad Sci U S A 97(12):6658-63
Tanner KG, et al.  (2000) Silent information regulator 2 family of NAD- dependent histone/protein deacetylases generates a unique product, 1-O-acetyl-ADP-ribose. Proc Natl Acad Sci U S A 97(26):14178-82
Freeman-Cook LL, et al.  (1999) The Schizosaccharomyces pombe hst4(+) gene is a SIR2 homologue with silencing and centromeric functions. Mol Biol Cell 10(10):3171-86