STI1 Hsp90 cochaperone STI1 [Saccharomyces cerevisiae S288C] - Gene

Summary

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Official Symbol: STI1
Official Full Name: Hsp90 cochaperone STI1
Primary source: SGD:S000005553
Locus tag: YOR027W
See related: AllianceGenome:SGD:S000005553; FungiDB:YOR027W; VEuPathDB:YOR027W
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 ATPase inhibitor activity; heat shock protein binding activity; and mRNA binding activity. Involved in protein folding and protein targeting to mitochondrion. Located in cytoplasm. Orthologous to human STIP1 (stress induced phosphoprotein 1). [provided by Alliance of Genome Resources, Nov 2024]
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Genomic context

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See STI1 in Genome Data Viewer

Location:: chromosome: XV

Exon count:: 1

Sequence:: Chromosome: XV; NC_001147.6 (381053..382822)

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 Hsp70-Hsp90 co-chaperone Hop/Stip1 shifts the proteostatic balance from folding towards degradation.
Title: The Hsp70-Hsp90 co-chaperone Hop/Stip1 shifts the proteostatic balance from folding towards degradation.
Data suggest that Sti1 regulates Hsp90 to coordinate transfer of clients from Hsp70 with advancement of the Hsp90 cycle. Binding of Sti1 to Hsp90 both prevents commitment to subsequent steps until a productive interaction with Hsp70- delivered clients has occurred and positions Hsp90 to advance in its cycle promptly after client delivery.
Title: Dual Roles for Yeast Sti1/Hop in Regulating the Hsp90 Chaperone Cycle.
Using a presequence-containing model protein and a site-directed photo-crosslinking approach, we identified the cytosolic chaperones Hsp70 (Ssa1) and Hsp90 (Hsp82) as well as their cochaperones, Sti1 and Ydj1, as putative cytosolic factors involved in mitochondrial protein import.
Title: The cytosolic cochaperone Sti1 is relevant for mitochondrial biogenesis and morphology.
Sti1 is a dynamic, elongated protein that consists of a flexible N-terminal module, a long linker and a rigid C-terminal module. Binding of Hsp90 and Hsp70 regulates the Sti1 conformation.
Title: Hsp90 regulates the dynamics of its cochaperone Sti1 and the transfer of Hsp70 between modules.
findings point to crucial roles of Hsp70, Sti1, and Hsp90 for efficient curing by overexpressed Hsp104 and provide evidence supporting the earlier suggestion that destruction of prions by protein disaggregation does not adequately explain the curing
Title: Sti1 regulation of Hsp70 and Hsp90 is critical for curing of Saccharomyces cerevisiae [PSI+] prions by Hsp104.
Neither Sti1 nor Cpr7 is necessary for prion propagation but the authors show that deletion of the STI1 and CPR7 genes leads to a significant reduction in the generation of [psi(-)] cells by Hsp104 overexpression.
Title: Hsp70/Hsp90 co-chaperones are required for efficient Hsp104-mediated elimination of the yeast [PSI(+)] prion but not for prion propagation.

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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 ATPase inhibitor activity	IDA Inferred from Direct Assay more info	PubMed
enables Hsp70 protein binding	IDA Inferred from Direct Assay more info	PubMed
enables Hsp90 protein binding	IBA Inferred from Biological aspect of Ancestor more info
enables Hsp90 protein binding	IDA Inferred from Direct Assay more info	PubMed
enables mRNA binding	IDA Inferred from Direct Assay more info	PubMed

Process	Evidence Code	Pubs
involved_in protein folding	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in protein localization	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in protein targeting to mitochondrion	IMP Inferred from Mutant Phenotype more info	PubMed

Component	Evidence Code	Pubs
located_in cytoplasm	IEA Inferred from Electronic Annotation more info
located_in cytoplasm	IPI Inferred from Physical Interaction more info	PubMed

General protein information

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Preferred Names: Hsp90 cochaperone STI1

NP_014670.1

Evolutionarily-conserved Hsp90 cochaperone; regulates spatial organization of amyloid-like proteins in the cytosol, thereby buffering the proteotoxicity caused by amyloid-like proteins; interacts with the Ssa group of the cytosolic Hsp70 chaperones and activates Ssa1p ATPase activity; interacts with Hsp90 chaperones and inhibits their ATPase activity; homolog of mammalian Hop

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

381053..382822

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GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NM_001183446.1 → NP_014670.1 TPA: Hsp90 cochaperone STI1 [Saccharomyces cerevisiae S288C]

See identical proteins and their annotated locations for NP_014670.1

Status: REVIEWED

UniProtKB/Swiss-Prot

D6W293, P15705

UniProtKB/TrEMBL

G2WMQ8, N1NY83

Conserved Domains (4) summary

PLN03088
Location:396 → 549

PLN03088; SGT1, suppressor of G2 allele of SKP1; Provisional

TIGR00990
Location:203 → 573

3a0801s09; mitochondrial precursor proteins import receptor (72 kDa mitochondrial outermembrane protein) (mitochondrial import receptor for the ADP/ATP carrier) (translocase of outermembrane tom70)

sd00006
Location:5 → 33

TPR; TPR repeat [structural motif]

pfam17830
Location:527 → 581

STI1; STI1 domain