SSB1 Hsp70 family ATPase SSB1 [Saccharomyces cerevisiae S288C] - Gene

Summary

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Official Symbol: SSB1
Official Full Name: Hsp70 family ATPase SSB1
Primary source: SGD:S000002388
Locus tag: YDL229W
See related: AllianceGenome:SGD:S000002388; FungiDB:YDL229W; VEuPathDB:YDL229W
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: YG101
Summary: Enables ATP hydrolysis activity; calmodulin binding activity; and unfolded protein binding activity. Involved in gene expression; regulation of translational fidelity; and ribosomal subunit export from nucleus. Located in cytoplasm. [provided by Alliance of Genome Resources, Nov 2024]
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Genomic context

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See SSB1 in Genome Data Viewer

Location:: chromosome: IV

Exon count:: 1

Sequence:: Chromosome: IV; NC_001136.10 (44065..45906)

Chromosome IV - NC_001136.10 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_001136.10

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Pathway of Hsp70 interactions at the ribosome.
Title: Pathway of Hsp70 interactions at the ribosome.
Cooperativity between the Ribosome-Associated Chaperone Ssb/RAC and the Ubiquitin Ligase Ltn1 in Ubiquitination of Nascent Polypeptides.
Title: Cooperativity between the Ribosome-Associated Chaperone Ssb/RAC and the Ubiquitin Ligase Ltn1 in Ubiquitination of Nascent Polypeptides.
Activity of the yeast cytoplasmic Hsp70 nucleotide-exchange factor Fes1 is regulated by reversible methionine oxidation.
Title: Activity of the yeast cytoplasmic Hsp70 nucleotide-exchange factor Fes1 is regulated by reversible methionine oxidation.
A positively charged region in the alpha-helical lid domain of SSB is identified. It is strictly required for ribosome binding. Crosslinking shows that Ssb binds close to the tunnel exit via contacts with both, ribosomal proteins and rRNA, and that specific contacts can be correlated with switching between the open (ATP-bound) and closed (ADP-bound) conformation.
Title: Interaction of the cotranslational Hsp70 Ssb with ribosomal proteins and rRNA depends on its lid domain.
Data show that the absence of either Ssb1/2 or Sch9 causes enhanced ribosome aggregation.
Title: The Hsp70 homolog Ssb affects ribosome biogenesis via the TORC1-Sch9 signaling pathway.
Study reveals molecular features of chaperone action during translation in eukaryotes by providing proteome-wide Ssb (two isoforms Ssb1 and Ssb2) interaction profiles with nascent chains at near-codon resolution. The Ssb interactome is broader than previously thought and includes nascent mitochondrial and endoplasmic reticulum- (ER) translocated proteins.
Title: Profiling Ssb-Nascent Chain Interactions Reveals Principles of Hsp70-Assisted Folding.
the ribosome-associated Hsp70 Ssb is redistributed away from Sup35 prion aggregates to the nascent chains, leading to an array of aggregation phenotypes that can mimic both overexpression and deletion of Ssb.
Title: Prion-Associated Toxicity is Rescued by Elimination of Cotranslational Chaperones.
Studied deletions of two major chaperone proteins, SSA1 and SSB1, from the HSP70 chaperone network in Sacchromyces cerevisiae.
Title: Quantitative proteomics and network analysis of SSA1 and SSB1 deletion mutants reveals robustness of chaperone HSP70 network in Saccharomyces cerevisiae.
Study finds that SSB (i.e. closely related isoforms Ssb1 and Ssb2) binds to a subset of nascent polypeptides whose intrinsic properties and slow translation rates hinder efficient cotranslational folding.
Title: The cotranslational function of ribosome-associated Hsp70 in eukaryotic protein homeostasis.
The ribosome-bound chaperone system consisting of the ribosome-associated complex (RAC) and the Hsp70 homologs SSB1 and SSB2 are required to stabilize translationally repressed ribosome-polylysine protein complexes.
Title: Ribosome-associated complex and Ssb are required for translational repression induced by polylysine segments within nascent chains.

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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 ATP binding	IEA Inferred from Electronic Annotation more info
enables ATP hydrolysis activity	IBA Inferred from Biological aspect of Ancestor more info
enables ATP hydrolysis activity	IDA Inferred from Direct Assay more info	PubMed
enables ATP hydrolysis activity	IEA Inferred from Electronic Annotation more info
enables ATP-dependent H2AZ histone chaperone activity	IEA Inferred from Electronic Annotation more info
enables ATP-dependent H3-H4 histone complex chaperone activity	IEA Inferred from Electronic Annotation more info
enables ATP-dependent protein folding chaperone	IEA Inferred from Electronic Annotation more info
enables DNA clamp loader activity	IEA Inferred from Electronic Annotation more info
enables calmodulin binding	IDA Inferred from Direct Assay more info	PubMed
enables chromatin extrusion motor activity	IEA Inferred from Electronic Annotation more info
enables cohesin loader activity	IEA Inferred from Electronic Annotation more info
enables heat shock protein binding	IBA Inferred from Biological aspect of Ancestor more info
enables hydrolase activity	IEA Inferred from Electronic Annotation more info
enables protein folding chaperone	IBA Inferred from Biological aspect of Ancestor more info
enables unfolded protein binding	IDA Inferred from Direct Assay more info	PubMed

Process	Evidence Code	Pubs
involved_in 'de novo' cotranslational protein folding	IDA Inferred from Direct Assay more info	PubMed
involved_in chaperone cofactor-dependent protein refolding	IBA Inferred from Biological aspect of Ancestor more info
involved_in chromatin looping	IEA Inferred from Electronic Annotation more info
involved_in chromatin remodeling	IEA Inferred from Electronic Annotation more info
involved_in cytoplasmic translation	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in cytoplasmic translation	IPI Inferred from Physical Interaction more info	PubMed
involved_in protein refolding	IBA Inferred from Biological aspect of Ancestor more info
involved_in rRNA processing	IGI Inferred from Genetic Interaction more info	PubMed
involved_in regulation of translational fidelity	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in ribosomal subunit export from nucleus	IGI Inferred from Genetic Interaction more info	PubMed
involved_in translation	IEA Inferred from Electronic Annotation more info
involved_in translational frameshifting	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in translational termination	IMP Inferred from Mutant Phenotype more info	PubMed

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

General protein information

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Preferred Names: Hsp70 family ATPase SSB1

NP_010052.1

EC 3.6.4.10

Cytoplasmic ATPase that is a ribosome-associated molecular chaperone; functions with J-protein partner Zuo1p; may be involved in folding of newly-made polypeptide chains; member of the HSP70 family; interacts with phosphatase subunit Reg1p; SSB1 has a paralog, SSB2, that arose from the whole genome duplication