| The Histone Deacetylases Hst1 and Rpd3 Integrate De Novo NAD[+] Metabolism with Phosphate Sensing in Saccharomyces cerevisiae. | The Histone Deacetylases Hst1 and Rpd3 Integrate De Novo NAD(+) Metabolism with Phosphate Sensing in Saccharomyces cerevisiae.
Groth B, Lee YC, Huang CC, McDaniel M, Huang K, Lee LH, Lin SJ., Free PMC Article | 06/7/2023 |
| The histone deacetylases Rpd3 and Hst1 antagonistically regulate de novo NAD(+) metabolism in the budding yeast Saccharomyces cerevisiae. | The histone deacetylases Rpd3 and Hst1 antagonistically regulate de novo NAD(+) metabolism in the budding yeast Saccharomyces cerevisiae.
Groth B, Huang CC, Lin SJ., Free PMC Article | 11/12/2022 |
| ChIP experiments with the BNA2 promoter indicated that Mac1 works with Hst1-containing repressor complexes to silence BNA expression. | The copper-sensing transcription factor Mac1, the histone deacetylase Hst1, and nicotinic acid regulate de novo NAD(+) biosynthesis in budding yeast.
James Theoga Raj C, Croft T, Venkatakrishnan P, Groth B, Dhugga G, Cater T, Lin SJ., Free PMC Article | 10/19/2019 |
| In the absence of Set1, there is loss of the DNA-binding transcriptional regulator Sum1 and the associated histone deacetylase Hst1 from chromatin in a locus-specific manner | Repression of Middle Sporulation Genes in Saccharomyces cerevisiae by the Sum1-Rfm1-Hst1 Complex Is Maintained by Set1 and H3K4 Methylation.
Jaiswal D, Jezek M, Quijote J, Lum J, Choi G, Kulkarni R, Park D, Green EM., Free PMC Article | 07/21/2018 |
| 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 | HST1 increases replicative lifespan of a sir2Δ mutant in the absence of PDE2 in Saccharomyces cerevisiae.
Kang WK, Devare M, Kim JY. | 03/11/2017 |
| 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 | Crystallization and preliminary crystallographic studies of the NAD+-dependent deacetylase HST1 from Saccharomyces cerevisiae.
Zhu Y, Teng M, Li X., Free PMC Article | 03/17/2012 |
| Sir2 and Hst1 subfunctionalized by acquiring complementary inactivating mutations in these interaction domains. | The duplicated deacetylases Sir2 and Hst1 subfunctionalized by acquiring complementary inactivating mutations.
Froyd CA, Rusche LN., Free PMC Article | 11/12/2011 |
| 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. | The budding yeast protein Sum1 functions independently of its binding partners Hst1 and Sir2 histone deacetylases to regulate microtubule assembly.
Sarkar S, Haldar S, Hajra S, Sinha P. | 11/27/2010 |
| 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. | Thiamine biosynthesis in Saccharomyces cerevisiae is regulated by the NAD+-dependent histone deacetylase Hst1.
Li M, Petteys BJ, McClure JM, Valsakumar V, Bekiranov S, Frank EL, Smith JS., Free PMC Article | 07/26/2010 |
| The results of this study suggest recruitment of the Sum1/Rfm1/Hst1 complex to a number of yeast origins, where Hst1 deacetylated H4 K5. | Control of replication initiation by the Sum1/Rfm1/Hst1 histone deacetylase.
Weber JM, Irlbacher H, Ehrenhofer-Murray AE., Free PMC Article | 01/21/2010 |
| Sir2p and Hst1p are paralogs with non-overlapping functions that can provide genetic robustness against null mutations through a substitution mechanism. | Substitution as a mechanism for genetic robustness: the duplicated deacetylases Hst1p and Sir2p in Saccharomyces cerevisiae.
Hickman MA, Rusche LN., Free PMC Article | 01/21/2010 |
| The differences in the silencing and repression functions of Sir2 and Hst1 may not be due to differences in enzymatic activities of the proteins but rather may be the result of distinct cofactor specificities. | Swapping the gene-specific and regional silencing specificities of the Hst1 and Sir2 histone deacetylases.
Mead J, McCord R, Youngster L, Sharma M, Gartenberg MR, Vershon AK., Free PMC Article | 01/21/2010 |