HST1 cDNA ORF clone, Saccharomyces cerevisiae S288C

The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.
Dujon B, Albermann K, Aldea M, Alexandraki D, Ansorge W, Arino J, Benes V, Bohn C, Bolotin-Fukuhara M, Bordonn? R, Boyer J, Camasses A, Casamayor A, Casas C, Ch?ret G, Cziepluch C, Daignan-Fornier B, Dang DV, de Haan M, Delius H, Durand P, Fairhead C, Feldmann H, Gaillon L, Kleine K
Nature387(6632 Suppl)98-102(1997 May)

Life with 6000 genes.
Goffeau A, Barrell BG, Bussey H, Davis RW, Dujon B, Feldmann H, Galibert F, Hoheisel JD, Jacq C, Johnston M, Louis EJ, Mewes HW, Murakami Y, Philippsen P, Tettelin H, Oliver SG
Science (New York, N.Y.)274(5287)546, 563-7(1996 Oct)

study demonstrates that Hst1, the closest Sir2 paralogue, deacetylates the acetylated lysine 16 of histone H4 (H4K16Ac) and represses PMA1 transcription in the sir2Delta pde2Delta mutant. Collectively,results suggest that Hst1 can substitute for Sir2 by deacetylating H4K16Ac only in the sir2Delta pde2Delta
Title: HST1 increases replicative lifespan of a sir2? mutant in the absence of PDE2 in Saccharomyces cerevisiae.

Crystals of HST1 grown by the hanging-drop vapour-diffusion method diffracted to 2.90 A resolution and belonged to space group P2(1), with unit-cell parameters a = 40.2, b = 101.7, c = 43.9 A, beta = 103.9 degrees
Title: Crystallization and preliminary crystallographic studies of the NAD+-dependent deacetylase HST1 from Saccharomyces cerevisiae.

Sir2 and Hst1 subfunctionalized by acquiring complementary inactivating mutations in these interaction domains.
Title: The duplicated deacetylases Sir2 and Hst1 subfunctionalized by acquiring complementary inactivating mutations.

These observations suggest that Sum1p is a novel regulator of microtubule function and as such, works independently from its binding partners Hst1 and Sir2 histone deacetylases.
Title: The budding yeast protein Sum1 functions independently of its binding partners Hst1 and Sir2 histone deacetylases to regulate microtubule assembly.

Data show that multiple thiamine (THI) genes in Saccharomyces cerevisiae are also regulated by the intracellular NAD(+) concentration via the NAD(+)-dependent histone deacetylase (HDAC) Hst1 and, to a lesser extent, Sir2.
Title: Thiamine biosynthesis in Saccharomyces cerevisiae is regulated by the NAD+-dependent histone deacetylase Hst1.