HST2/YPL015C Literature Guide Help

Other names published for HST2: YPL015C

HST2 - Substrates/Ligands/Cofactors (19)

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
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
Liang Z, et al.  (2010) Investigation of the Catalytic Mechanism of Sir2 Enzyme with QM/MM Approach: SN1 vs SN2? J Phys Chem B 114(36):11927-33
Sanders BD, et al.  (2010) Structural basis for sirtuin function: What we know and what we don't. Biochim Biophys Acta 1804(8):1604-1616
Sanders BD, et al.  (2009) Identification and characterization of novel sirtuin inhibitor scaffolds. Bioorg Med Chem 17(19):7031-41
Wang CL, et al.  (2008) A yeast sir2 mutant temperature sensitive for silencing. Genetics 180(4):1955-62
Sanders BD, et al.  (2007) Structural basis for nicotinamide inhibition and base exchange in Sir2 enzymes. Mol Cell 25(3):463-72
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
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
Schmidt MT, et al.  (2004) Coenzyme specificity of Sir2 protein deacetylases: implications for physiological regulation. J Biol Chem 279(38):40122-9
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
North BJ, et al.  (2003) The human Sir2 ortholog, SIRT2, is an NAD+-dependent tubulin deacetylase. Mol Cell 11(2):437-44
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
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