YDJ1 type I HSP40 co-chaperone YDJ1 [Saccharomyces cerevisiae S288C] - Gene

Summary

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Official Symbol: YDJ1
Official Full Name: type I HSP40 co-chaperone YDJ1
Primary source: SGD:S000005008
Locus tag: YNL064C
See related: AllianceGenome:SGD:S000005008; FungiDB:YNL064C; VEuPathDB:YNL064C
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: HSP40; MAB3; MAS5
Summary: Enables ATPase activator activity and unfolded protein binding activity. Involved in several processes, including protein folding; protein targeting; and proteolysis involved in protein catabolic process. Located in cytosol and perinuclear region of cytoplasm. Part of TRC complex. Used to study Alzheimer's disease. Orthologous to several human genes including DNAJA2 (DnaJ heat shock protein family (Hsp40) member A2). [provided by Alliance of Genome Resources, Dec 2024]
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Genomic context

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See YDJ1 in Genome Data Viewer

Location:: chromosome: XIV

Exon count:: 1

Sequence:: Chromosome: XIV; NC_001146.8 (505868..507097, complement)

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?

Ydj1 interaction at nucleotide-binding-domain of yeast Ssa1 impacts Hsp90 collaboration and client maturation.
Title: Ydj1 interaction at nucleotide-binding-domain of yeast Ssa1 impacts Hsp90 collaboration and client maturation.
Spatial sequestration of misfolded proteins as an active chaperone-mediated process during heat stress.
Title: Spatial sequestration of misfolded proteins as an active chaperone-mediated process during heat stress.
The Yeast Hsp70 Cochaperone Ydj1 Regulates Functional Distinction of Ssa Hsp70s in the Hsp90 Chaperoning Pathway.
Title: The Yeast Hsp70 Cochaperone Ydj1 Regulates Functional Distinction of Ssa Hsp70s in the Hsp90 Chaperoning Pathway.
this study shows that cytosolic Hsp70 chaperones and their Hsp40 cochaperones Ydj1 and Sis1 interact with newly synthesized beta-barrel proteins.
Title: Cytosolic Hsp70 and Hsp40 chaperones enable the biogenesis of mitochondrial β-barrel proteins.
Saccharomyces cerevisiae Hsp40 Ydj1p is isoprenylated but not subject to additional modification. In fact, additional modifications are detrimental to Ydj1p activity in vivo We have taken advantage of the properties of Ydj1p and a Ydj1p-dependent growth assay to identify sequences that permit Ydj1p isoprenylation in vivo while simultaneously selecting against nonprenylatable and more extensively modified sequences.
Title: Protein Isoprenylation in Yeast Targets COOH-Terminal Sequences Not Adhering to the CaaX Consensus.
The authors provide genetic, biochemical, and biophysical evidence that the Ydj1p CaaX motif is isoprenylated but not cleaved and carboxylmethylated.
Title: A shunt pathway limits the CaaX processing of Hsp40 Ydj1p and regulates Ydj1p-dependent phenotypes.
Gcn5, Snf2, and Ydj1 cooperate in eviction of promoter nucleosomes genome-wide, achieving robust transcription of the most highly expressed subset of genes in yeast.
Title: Genome-wide cooperation by HAT Gcn5, remodeler SWI/SNF, and chaperone Ydj1 in promoter nucleosome eviction and transcriptional activation.
Ydj1 is required for the formation of Dhh1 complexes.
Title: Proteomic Analysis of Dhh1 Complexes Reveals a Role for Hsp40 Chaperone Ydj1 in Yeast P-Body Assembly.
Ydj1 directs disaggregation activity of the Hsp100-based machinery to provide stress protection.
Title: Hsp40s specify functions of Hsp104 and Hsp90 protein chaperone machines.
The chaperone Ydj1 interacts specifically with mutant septins during septin quality control.
Title: Cytosolic chaperones mediate quality control of higher-order septin assembly in budding yeast.

Submit: New GeneRIF Correction See all GeneRIFs (29)

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 ATP binding	IEA Inferred from Electronic Annotation more info
enables ATPase activator activity	IDA Inferred from Direct Assay more info	PubMed
enables Hsp70 protein binding	IEA Inferred from Electronic Annotation more info
enables metal ion binding	IEA Inferred from Electronic Annotation more info
enables protein-folding chaperone binding	IBA Inferred from Biological aspect of Ancestor more info
enables unfolded protein binding	IDA Inferred from Direct Assay more info	PubMed
enables unfolded protein binding	IEA Inferred from Electronic Annotation more info
enables zinc ion binding	RCA inferred from Reviewed Computational Analysis more info	PubMed

Process	Evidence Code	Pubs
involved_in 'de novo' protein folding	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in ERAD pathway	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in cellular response to heat	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in cellular response to starvation	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in protein folding	IEA Inferred from Electronic Annotation more info
involved_in protein refolding	IBA Inferred from Biological aspect of Ancestor more info
involved_in protein refolding	IDA Inferred from Direct Assay more info	PubMed
involved_in protein targeting to ER	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in protein targeting to mitochondrion	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in protein transport	IEA Inferred from Electronic Annotation more info
involved_in response to heat	IEA Inferred from Electronic Annotation more info
involved_in tRNA import into nucleus	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in ubiquitin-dependent protein catabolic process	IMP Inferred from Mutant Phenotype more info	PubMed

Component	Evidence Code	Pubs
part_of TRC complex	IDA Inferred from Direct Assay 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 cytosol	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
is_active_in nucleus	IBA Inferred from Biological aspect of Ancestor more info
located_in perinuclear region of cytoplasm	IDA Inferred from Direct Assay more info	PubMed
located_in perinuclear region of cytoplasm	IEA Inferred from Electronic Annotation more info

General protein information

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Preferred Names: type I HSP40 co-chaperone YDJ1

NP_014335.1

Type I HSP40 co-chaperone; regulates HSP90 and HSP70 functions; acts as an adaptor that helps Rsp5p recognize and ubiquitinate misfolded, cytosolic proteins after heat shock; critical for determining cell size at Start as a function of growth rate; involved in protein translocation across membranes; forms cytotoxic amyloidogenic-like structures in vitro; DnaJ family member; chimeric protein in which the human p58IPK J domain replaces the yeast Ydj1p J domain can complement yeast ydj1 mutant

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

505868..507097 complement

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GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NM_001182902.1 → NP_014335.1 TPA: type I HSP40 co-chaperone YDJ1 [Saccharomyces cerevisiae S288C]

See identical proteins and their annotated locations for NP_014335.1

Status: REVIEWED

UniProtKB/Swiss-Prot

D6W1B6, P25491

UniProtKB/TrEMBL

C7GLT9, N1NWM8

Conserved Domains (1) summary

COG0484
Location:2 → 368

DnaJ; DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational modification, protein turnover, chaperones]