SSB2 Hsp70 family ATPase SSB2 [Saccharomyces cerevisiae S288C] - Gene

Summary

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Official Symbol: SSB2
Official Full Name: Hsp70 family ATPase SSB2
Primary source: SGD:S000005153
Locus tag: YNL209W
See related: AllianceGenome:SGD:S000005153; FungiDB:YNL209W; VEuPathDB:YNL209W
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: YG103
Summary: Enables ATP hydrolysis activity and unfolded protein binding activity. Involved in several processes, including cellular response to glucose starvation; gene expression; and ribosomal subunit export from nucleus. Located in cytoplasmic stress granule and plasma membrane. [provided by Alliance of Genome Resources, Dec 2024]
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Genomic context

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See SSB2 in Genome Data Viewer

Location:: chromosome: XIV

Exon count:: 1

Sequence:: Chromosome: XIV; NC_001146.8 (252059..253900)

Chromosome XIV - NC_001146.8 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_001146.8

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

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.
These findings suggest that Ssb2 is a critical factor that modulates Gcn4 functions in the nucleus and cytosol.
Title: Ssb2 is a novel factor in regulating synthesis and degradation of Gcn4 in Saccharomyces cerevisiae.
SSB2 is involved in the endoplasmic reticulum stress response.
Title: Yeast molecular chaperone gene SSB2 is involved in the endoplasmic reticulum stress response.
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.
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.
Zuo1 and Ssz1 together with the Hsp70 homolog Ssb1/2 form a functional triad involved in translation and early polypeptide folding processes.
Title: Functional characterization of the atypical Hsp70 subunit of yeast ribosome-associated complex.
A plausible role of the Ssb2 chaperone is to stabilize genetic networks, thus making them more tolerant to malfunctioning of their constituents.
Title: Why molecular chaperones buffer mutational damage: a case study with a yeast Hsp40/70 system.
Results suggest that RAC and Ssb1/2p are crucial in maintaining translational fidelity beyond their postulated role as chaperones for nascent polypeptides.
Title: The ribosome-bound chaperones RAC and Ssb1/2p are required for accurate translation in Saccharomyces cerevisiae.

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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 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 cellular response to glucose starvation	IGI Inferred from Genetic Interaction 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

Component	Evidence Code	Pubs
located_in cytoplasm	HDA more info	PubMed
is_active_in cytoplasm	IBA Inferred from Biological aspect of Ancestor more info
located_in cytoplasm	IEA Inferred from Electronic Annotation more info
located_in cytoplasmic stress granule	HDA more info	PubMed
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 SSB2

NP_014190.1

EC 3.6.4.10

Cytoplasmic ATPase that is a ribosome-associated molecular chaperone; functions with J-protein partner Zuo1p; may be involved in the folding of newly-synthesized polypeptide chains; member of the HSP70 family; SSB2 has a paralog, SSB1, 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_001146.8 Reference assembly

Range

252059..253900

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GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NM_001183047.1 → NP_014190.1 TPA: Hsp70 family ATPase SSB2 [Saccharomyces cerevisiae S288C]

See identical proteins and their annotated locations for NP_014190.1

Status: REVIEWED

UniProtKB/Swiss-Prot

D6W0Y1, P40150

UniProtKB/TrEMBL

A6ZRN1, B3LP53, G2WLQ4

Conserved Domains (1) summary

PTZ00009
Location:6 → 575

PTZ00009; heat shock 70 kDa protein; Provisional