HSP12 lipid-binding protein HSP12 [Saccharomyces cerevisiae S288C] - Gene

Summary

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Official Symbol: HSP12
Official Full Name: lipid-binding protein HSP12
Primary source: SGD:S000001880
Locus tag: YFL014W
See related: AllianceGenome:SGD:S000001880; FungiDB:YFL014W; VEuPathDB:YFL014W
Gene type: protein coding
RefSeq status: REVIEWED
Organism: Saccharomyces cerevisiae S288C (strain: S288C)
Lineage: Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces
Also known as: GLP1; HOR5
Summary: Enables lipid binding activity. Involved in several processes, including cellular response to heat; cellular response to osmotic stress; and cellular response to oxidative stress. Located in cytosol; endosome; and plasma membrane. [provided by Alliance of Genome Resources, Oct 2024]
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Genomic context

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See HSP12 in Genome Data Viewer

Location:: chromosome: VI

Exon count:: 1

Sequence:: Chromosome: VI; NC_001138.5 (107256..107585)

Chromosome VI - NC_001138.5 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_001138.5

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Chromatin conformations of HSP12 during transcriptional activation in the Saccharomyces cerevisiae stationary phase.
Title: Chromatin conformations of HSP12 during transcriptional activation in the Saccharomyces cerevisiae stationary phase.
PiP2 favors an alpha-helical structure of non-recombinant Hsp12 of Saccharomyces cerevisiae.
Title: PiP(2) favors an α-helical structure of non-recombinant Hsp12 of Saccharomyces cerevisiae.
Using the anhydrobiote, budding yeast, the authors show that trehalose and Hsp12, a small intrinsically disordered protein (sIDP) of the hydrophilin family, synergize to mitigate completely the inviability caused by the lethal stresses of desiccation.
Title: Synergy between the small intrinsically disordered protein Hsp12 and trehalose sustain viability after severe desiccation.
these results demonstrate that the combined action of Hsp12p, Pau5p and a killer toxin is sufficient to steer a yeast community.
Title: Hsp12p and PAU genes are involved in ecological interactions between natural yeast strains.
Hsp12 expression contributes to lifespan extension, possibly via membrane alterations
Title: NMR structure of Hsp12, a protein induced by and required for dietary restriction-induced lifespan extension in yeast.
NMR spectra collected in presence of paramagnetic spin relaxation agents (5DSA, 16DSA, and Gd(DTPA-BMA)) indicated that the amphipathic alpha-helices of Hsp12 in SDS micelles lie on the membrane surface.
Title: Structural characterization of Hsp12, the heat shock protein from Saccharomyces cerevisiae, in aqueous solution where it is intrinsically disordered and in detergent micelles where it is locally α-helical.
Hsp12 is completely unfolded; however, in the presence of certain lipids, it adopts a helical structure. The presence of Hsp12 does not alter the overall lipid composition of the plasma membrane but increases membrane stability.
Title: Hsp12 is an intrinsically unstructured stress protein that folds upon membrane association and modulates membrane function.
The decrease of the turgor pressure in the case of WT strain upon addition of Congo red is shown to be consistent with an upregulation of Hsp12p in the close vicinity of the plasma membrane.
Title: The role of the heat shock protein Hsp12p in the dynamic response of Saccharomyces cerevisiae to the addition of Congo red.
Hsp12 contributes to yeast tolerance to freezing stress. Hsp12p plays a role in freezing tolerance in a way that seems to be interchangeable with trehalose.
Title: Small heat-shock protein Hsp12 contributes to yeast tolerance to freezing stress.
Hsp12p played a role in maintaining plasma membrane integrity during applied oxidative stress.
Title: A compensatory increase in trehalose synthesis in response to desiccation stress in Saccharomyces cerevisiae cells lacking the heat shock protein Hsp12p.

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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 lipid binding	IBA Inferred from Biological aspect of Ancestor more info
enables lipid binding	IDA Inferred from Direct Assay more info	PubMed

Process	Evidence Code	Pubs
involved_in cell adhesion	IDA Inferred from Direct Assay more info	PubMed
involved_in cellular response to heat	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in cellular response to osmotic stress	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in cellular response to oxidative stress	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in plasma membrane organization	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in protein folding	IEA Inferred from Electronic Annotation more info

Component	Evidence Code	Pubs
located_in cytoplasm	HDA more info	PubMed
is_active_in cytosol	IBA Inferred from Biological aspect of Ancestor more info
located_in cytosol	IDA Inferred from Direct Assay more info	PubMed
located_in endosome	IDA Inferred from Direct Assay more info	PubMed
located_in nucleus	HDA more info	PubMed
located_in plasma membrane	HDA more info	PubMed
is_active_in plasma membrane	IBA Inferred from Biological aspect of Ancestor more info
located_in plasma membrane	IDA Inferred from Direct Assay more info	PubMed

General protein information

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Preferred Names: lipid-binding protein HSP12

NP_116640.1

Plasma membrane protein involved in maintaining membrane organization; involved in maintaining organization during stress conditions; induced by heat shock, oxidative stress, osmostress, stationary phase, glucose depletion, oleate and alcohol; protein abundance increased in response to DNA replication stress and dietary restriction; regulated by the HOG and Ras-Pka pathways; required for dietary restriction-induced lifespan extension