SSE1 adenyl-nucleotide exchange factor SSE1 [Saccharomyces cerevisiae S288C] - Gene

Summary

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Official Symbol: SSE1
Official Full Name: adenyl-nucleotide exchange factor SSE1
Primary source: SGD:S000006027
Locus tag: YPL106C
See related: AllianceGenome:SGD:S000006027; FungiDB:YPL106C; VEuPathDB:YPL106C
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: LPG3; MSI3
Summary: Enables ATP binding activity; adenyl-nucleotide exchange factor activity; and peptide binding activity. Involved in autophagy; proteasomal protein catabolic process; and protein refolding. Located in cytoplasm. Human ortholog(s) of this gene implicated in Chagas disease. Orthologous to several human genes including HSPA4 (heat shock protein family A (Hsp70) member 4) and HSPH1 (heat shock protein family H (Hsp110) member 1). [provided by Alliance of Genome Resources, Dec 2024]
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Genomic context

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See SSE1 in Genome Data Viewer

Location:: chromosome: XVI

Exon count:: 1

Sequence:: Chromosome: XVI; NC_001148.4 (350194..352275, complement)

Chromosome XVI - NC_001148.4 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_001148.4

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Interdomain communication suppressing high intrinsic ATPase activity of Sse1 is essential for its co-disaggregase activity with Ssa1.
Title: Interdomain communication suppressing high intrinsic ATPase activity of Sse1 is essential for its co-disaggregase activity with Ssa1.
The Sse1/Hsp70 complex maintains the solubility of FLAG-Pgk1-300, thereby stimulating its Upf-dependent degradation by the proteasomes.
Title: Crucial role of ATP-bound Sse1 in Upf1-dependent degradation of the truncated product.
A key role for Sse1 (Hsp110), in cooperation with Hsp104, in regulating the length and assembly state of [PSI+] prion fibrils in vivo.
Title: Prion aggregate structure in yeast cells is determined by the Hsp104-Hsp110 disaggregase machinery.
cytosolic Hsp70 interacts with up to three types of nucleotide exchange factors (NEFs) homologous to human counterparts: Sse1/Sse2 (Heat shock protein 110 (Hsp110)), Fes1 (HspBP1), and Snl1 (Bag-1).
Title: Hierarchical functional specificity of cytosolic heat shock protein 70 (Hsp70) nucleotide exchange factors in yeast.
13 novel mutations in Sse1 have varying effects on both the ability of S. cerevisiae to propagate the [PSI+] prion and also to grow at increased temperatures.
Title: Mutational analysis of Sse1 (Hsp110) suggests an integral role for this chaperone in yeast prion propagation in vivo.
Studies indicate that Sse1 and Sse2 chaperones define the Hsp110 subclass of the Hsp70 chaperones.
Title: The control of spindle length by Hsp70 and Hsp110 molecular chaperones.
The role of Hsp110 Sse1 as a nucleotide exchange factor for the Hsp70 chaperones Ssa1/Ssa2 is required for maintaining proper distribution of kinesin-5 motors within the spindle, which is subsequently required for bipolar spindle assembly in S phase.
Title: Hsp110 is required for spindle length control.
Findings support a model in which Hsp110 chaperones control the fate of some client proteins by influencing the decision to fold or degrade as dictated by the Hsp70-Hsp90 chaperone environment.
Title: Hsp110 chaperones control client fate determination in the hsp70-Hsp90 chaperone system.
compare Grp170 Lhs1 with Hsp110 Sse1 and find that residues important for Sse1 nucleotide exchange factor (NEF) activity are conserved in Lhs1 and that mutations in these residues in Lhs1 compromise NEF activity
Title: The endoplasmic reticulum Grp170 acts as a nucleotide exchange factor of Hsp70 via a mechanism similar to that of the cytosolic Hsp110.
Sse1 exploits a Bag-1-like mechanism to catalyze nucleotide release, which involves opening of the Ssa1 NBD by tilting lobe II. Hsp110 proteins use a unique binding mode to catalyze nucleotide release from Hsp70s by a functionally convergent mechanism
Title: Insights into the structural dynamics of the Hsp110-Hsp70 interaction reveal the mechanism for nucleotide exchange activity.

Submit: New GeneRIF Correction See all GeneRIFs (20)

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 ATP binding	IDA Inferred from Direct Assay more info	PubMed
enables ATP binding	IEA Inferred from Electronic Annotation more info
enables ATP binding	IMP Inferred from Mutant Phenotype more info	PubMed
enables ATP-dependent protein folding chaperone	IEA Inferred from Electronic Annotation more info
enables adenyl-nucleotide exchange factor activity	IBA Inferred from Biological aspect of Ancestor more info
enables adenyl-nucleotide exchange factor activity	IDA Inferred from Direct Assay more info	PubMed
enables calmodulin binding	IEA Inferred from Electronic Annotation more info
enables peptide binding	IDA Inferred from Direct Assay more info	PubMed

Process	Evidence Code	Pubs
involved_in autophagy	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in proteasomal ubiquitin-independent protein catabolic process	IGI Inferred from Genetic Interaction more info	PubMed
involved_in proteasome-mediated ubiquitin-dependent protein catabolic process	IGI Inferred from Genetic Interaction more info	PubMed
involved_in protein folding	IBA Inferred from Biological aspect of Ancestor more info
involved_in protein folding	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in protein refolding	IDA Inferred from Direct Assay more info	PubMed

Component	Evidence Code	Pubs
located_in cytoplasm	HDA more info	PubMed
located_in cytoplasm	IEA Inferred from Electronic Annotation more info
is_active_in cytosol	IBA Inferred from Biological aspect of Ancestor more info
is_active_in nucleus	IBA Inferred from Biological aspect of Ancestor more info

General protein information

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Preferred Names: adenyl-nucleotide exchange factor SSE1

NP_015219.1

ATPase component of heat shock protein Hsp90 chaperone complex; serves as nucleotide exchange factor to load ATP onto the SSA class of cytosolic Hsp70s; plays a role in prion propagation and determining prion variants; binds unfolded proteins; member of Hsp110 subclass of HSP70 proteins; deletion results in spindle elongation in S phase; SSE1 has a paralog, SSE2, 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_001148.4 Reference assembly

Range

350194..352275 complement

Download

GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NM_001183920.1 → NP_015219.1 TPA: adenyl-nucleotide exchange factor SSE1 [Saccharomyces cerevisiae S288C]

See identical proteins and their annotated locations for NP_015219.1

Status: REVIEWED

UniProtKB/Swiss-Prot

D6W3R1, P32589

UniProtKB/TrEMBL

A6ZWE5, C7GJ60, N1NX50

Conserved Domains (1) summary

pfam00012
Location:4 → 644

HSP70; Hsp70 protein