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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Gene Review: 

HST2  -  histone deacetylase HST2

Saccharomyces cerevisiae S288c

Synonyms: Homologous to SIR2 protein 2, LPA2C, NAD-dependent protein deacetylase HST2, Regulatory protein SIR2 homolog 2, YPL015C
 
 
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High impact information on HST2

  • Structure and autoregulation of the yeast Hst2 homolog of Sir2 [1].
  • Kinetic studies further suggest that ADP-ribose inhibits the Hst2 reaction in a biologically relevant manner [2].
  • Here we use in vitro deacetylase assays and a variety of potential substrates to examine the substrate specificity of yeast homologue Hst2 [3].
  • This nuclear exclusion is mediated by the exportin chromosomal region maintenance 1 (Crm1) and a putative leucine-rich nuclear export sequence in Hst2, which overlaps a unique autoregulatory helix [4].
  • Structure of the yeast Hst2 protein deacetylase in ternary complex with 2'-O-acetyl ADP ribose and histone peptide [5].
 

Biological context of HST2

  • Here, we show that Hst2 moves between the nucleus and cytoplasm, but is largely cytoplasmic owing to efficient nuclear export [4].
 

Associations of HST2 with chemical compounds

 

Other interactions of HST2

  • HST2 mediates SIR2-independent life-span extension by calorie restriction [7].

References

  1. Structure and autoregulation of the yeast Hst2 homolog of Sir2. Zhao, K., Chai, X., Clements, A., Marmorstein, R. Nat. Struct. Biol. (2003) [Pubmed]
  2. Use of Substrate Analogs and Mutagenesis to Study Substrate Binding and Catalysis in the Sir2 Family of NAD-dependent Protein Deacetylases. Khan, A.N., Lewis, P.N. J. Biol. Chem. (2006) [Pubmed]
  3. Unstructured conformations are a substrate requirement for the Sir2 family of NAD-dependent protein deacetylases. Khan, A.N., Lewis, P.N. J. Biol. Chem. (2005) [Pubmed]
  4. Nuclear export modulates the cytoplasmic Sir2 homologue Hst2. Wilson, J.M., Le, V.Q., Zimmerman, C., Marmorstein, R., Pillus, L. EMBO Rep. (2006) [Pubmed]
  5. Structure of the yeast Hst2 protein deacetylase in ternary complex with 2'-O-acetyl ADP ribose and histone peptide. Zhao, K., Chai, X., Marmorstein, R. Structure (Camb.) (2003) [Pubmed]
  6. Short-chain fatty acid activation by acyl-coenzyme A synthetases requires SIR2 protein function in Salmonella enterica and Saccharomyces cerevisiae. Starai, V.J., Takahashi, H., Boeke, J.D., Escalante-Semerena, J.C. Genetics (2003) [Pubmed]
  7. HST2 mediates SIR2-independent life-span extension by calorie restriction. Lamming, D.W., Latorre-Esteves, M., Medvedik, O., Wong, S.N., Tsang, F.A., Wang, C., Lin, S.J., Sinclair, D.A. Science (2005) [Pubmed]
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