HST1 histone deacetylase HST1 [Saccharomyces cerevisiae S288C] - Gene

Summary

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Official Symbol: HST1
Official Full Name: histone deacetylase HST1
Primary source: SGD:S000005429
Locus tag: YOL068C
See related: AllianceGenome:SGD:S000005429; FungiDB:YOL068C; VEuPathDB:YOL068C
Gene type: protein coding
RefSeq status: REVIEWED
Organism: Saccharomyces cerevisiae S288C (strain: S288C)
Lineage: Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces
Summary: Enables NAD-dependent histone deacetylase activity and NAD-independent histone deacetylase activity. Involved in histone deacetylation; negative regulation of mitotic recombination; and silent mating-type cassette heterochromatin assembly. Part of Set3 complex. Human ortholog(s) of this gene implicated in Huntington's disease. Orthologous to human SIRT1 (sirtuin 1). [provided by Alliance of Genome Resources, Apr 2022]
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Genomic context

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Location:: chromosome: XV

Exon count:: 1

Sequence:: Chromosome: XV; NC_001147.6 (200368..201879, complement)

Chromosome XV - NC_001147.6 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_001147.6

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

The Histone Deacetylases Hst1 and Rpd3 Integrate De Novo NAD[+] Metabolism with Phosphate Sensing in Saccharomyces cerevisiae.
Title: The Histone Deacetylases Hst1 and Rpd3 Integrate De Novo NAD(+) Metabolism with Phosphate Sensing in Saccharomyces cerevisiae.
The histone deacetylases Rpd3 and Hst1 antagonistically regulate de novo NAD(+) metabolism in the budding yeast Saccharomyces cerevisiae.
Title: The histone deacetylases Rpd3 and Hst1 antagonistically regulate de novo NAD(+) metabolism in the budding yeast Saccharomyces cerevisiae.
ChIP experiments with the BNA2 promoter indicated that Mac1 works with Hst1-containing repressor complexes to silence BNA expression.
Title: The copper-sensing transcription factor Mac1, the histone deacetylase Hst1, and nicotinic acid regulate de novo NAD(+) biosynthesis in budding yeast.
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
Title: Repression of Middle Sporulation Genes in Saccharomyces cerevisiae by the Sum1-Rfm1-Hst1 Complex Is Maintained by Set1 and H3K4 Methylation.
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 sir2Δ 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.
The results of this study suggest recruitment of the Sum1/Rfm1/Hst1 complex to a number of yeast origins, where Hst1 deacetylated H4 K5.
Title: Control of replication initiation by the Sum1/Rfm1/Hst1 histone deacetylase.

Submit: New GeneRIF Correction See all GeneRIFs (12)

Pathways from PubChem

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Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Homology

Orthologs from OrthoDB

Gene Ontology Provided by SGD

Function	Evidence Code	Pubs
enables NAD+ binding	IBA Inferred from Biological aspect of Ancestor more info
enables NAD+ binding	IEA Inferred from Electronic Annotation more info
enables NAD-dependent histone H4K16 deacetylase activity	IBA Inferred from Biological aspect of Ancestor more info
enables NAD-dependent histone deacetylase activity	IDA Inferred from Direct Assay more info	PubMed
enables NAD-dependent histone deacetylase activity	IEA Inferred from Electronic Annotation more info
enables NAD-dependent protein lysine deacetylase activity	IEA Inferred from Electronic Annotation more info
enables metal ion binding	IEA Inferred from Electronic Annotation more info
enables transferase activity	IEA Inferred from Electronic Annotation more info
enables zinc ion binding	RCA inferred from Reviewed Computational Analysis more info	PubMed

Process	Evidence Code	Pubs
involved_in chromatin organization	IEA Inferred from Electronic Annotation more info
involved_in heterochromatin formation	IBA Inferred from Biological aspect of Ancestor more info
involved_in heterochromatin formation	IEA Inferred from Electronic Annotation more info
involved_in negative regulation of mitotic recombination	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in silent mating-type cassette heterochromatin formation	IGI Inferred from Genetic Interaction more info	PubMed
involved_in silent mating-type cassette heterochromatin formation	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in sporulation resulting in formation of a cellular spore	IEA Inferred from Electronic Annotation more info

Component	Evidence Code	Pubs
part_of Set3 complex	IDA Inferred from Direct Assay more info	PubMed
is_active_in nucleus	IBA Inferred from Biological aspect of Ancestor more info
located_in nucleus	IEA Inferred from Electronic Annotation more info

General protein information

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Preferred Names: histone deacetylase HST1

NP_014573.1

EC 2.3.1.286

NAD(+)-dependent histone deacetylase; essential subunit of the Sum1p/Rfm1p/Hst1p complex required for ORC-dependent silencing and meiotic repression; non-essential subunit of the Set3C deacetylase complex; involved in telomere maintenance; HST1 has a paralog, SIR2, that arose from the whole genome duplication

NCBI Reference Sequences (RefSeq)

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Genome Annotation

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference assembly

Genomic

NC_001147.6 Reference assembly

Range

200368..201879 complement

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GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NM_001183323.1 → NP_014573.1 TPA: histone deacetylase HST1 [Saccharomyces cerevisiae S288C]

See identical proteins and their annotated locations for NP_014573.1

Status: REVIEWED

UniProtKB/Swiss-Prot

D6W1Z9, P53685

UniProtKB/TrEMBL

A6ZNE2, B3LIZ2, B5VRI4, C7GK35, G2WMG6, N1P426

Conserved Domains (2) summary

cd01408
Location:201 → 461

SIRT1; Eukaryotic group (class1) which includes human sirtuins SIRT1-3 and yeast Hst1-4; and are members of the SIR2 family of proteins, silent information regulator 2 (Sir2) enzymes which catalyze NAD+-dependent protein/histone deacetylation. Sir2 proteins ...

pfam04574
Location:53 → 207

DUF592; Protein of unknown function (DUF592)