JAC1/YGL018C Summary Help

Standard Name JAC1 1
Systematic Name YGL018C
Feature Type ORF, Verified
Description Specialized J-protein that functions in Fe-S cluster biogenesis; functions with Hsp70 in Fe-S cluster biogenesis in mitochondria; involved in iron metabolism; contains a J domain typical to J-type chaperones; localizes to the mitochondrial matrix (2, 3, 4 and see Summary Paragraph)
Name Description J-type Accessory Chaperone 1
Chromosomal Location
ChrVII:459664 to 459110 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
Gbrowse
Gene Ontology Annotations All JAC1 GO evidence and references
  View Computational GO annotations for JAC1
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
High-throughput
Regulators 3 genes
Resources
Classical genetics
reduction of function
repressible
Large-scale survey
null
reduction of function
Resources
36 total interaction(s) for 30 unique genes/features.
Physical Interactions
  • Affinity Capture-RNA: 1
  • Affinity Capture-Western: 1
  • Biochemical Activity: 1
  • Co-purification: 1
  • Reconstituted Complex: 1

Genetic Interactions
  • Dosage Rescue: 3
  • Negative Genetic: 22
  • Phenotypic Suppression: 1
  • Positive Genetic: 1
  • Synthetic Growth Defect: 1
  • Synthetic Lethality: 1
  • Synthetic Rescue: 2

Resources
Expression Summary
histogram
Resources
Length (a.a.) 184
Molecular Weight (Da) 21,778
Isoelectric Point (pI) 8.4
Localization
Phosphorylation PhosphoGRID | PhosphoPep Database
Structure
Homologs
sequence information
ChrVII:459664 to 459110 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
SGD ORF map
Last Update Coordinates: 2011-02-03 | Sequence: 1996-07-31
Subfeature details
Relative
Coordinates
Chromosomal
Coordinates
Most Recent Updates
Coordinates Sequence
CDS 1..555 459664..459110 2011-02-03 1996-07-31
Retrieve sequences
Analyze Sequence
S288C only
S288C vs. other species
S288C vs. other strains
Resources
External Links All Associated Seq | Entrez Gene | Entrez RefSeq Protein | MIPS | Search all NCBI (Entrez) | UniProtKB
Primary SGDIDS000002986
SUMMARY PARAGRAPH for JAC1

Hsp40/DnaJ is a family of proteins, established by bacterial DnaJ, that regulates Hsp70 chaperone activity. Hsp40s stimulate the intrinsically weak ATPase activity of Hsp70 proteins and facilitate Hsp70 interaction with polypeptide substrates. Hsp70 family members often have multiple Hsp40 partners, and these specific pairings govern Hsp70 chaperone involvement in particular processes (reviewed in 5, 6, and 7). All Hsp40s contain a highly conserved 75-amino acid J domain, which interacts with the ATPase domain of Hsp70 to stimulate ATP hydrolysis. However, there are also other conserved structural domains, and based on the presence or absence of these regions, the Hsp40 family can be divided into three subtypes: type I, type II and type III (a comprehensive overview of the structural features of the different HSP40 subtypes can be found in 7). Sequence analysis of the S. cerevisiae genome has revealed 22 proteins in the Hsp40/DnaJ family: YDJ1, XDJ1, APJ1, SIS1, DJP1, ZUO1, SWA2, JJJ1, JJJ2, JJJ3, CAJ1, CWC23, MDJ1, MDJ2, PAM18, JAC1, JID1, SCJ1, HLJ1, JEM1, SEC63, and ERJ5 (7).

Last updated: 2006-12-19 Contact SGD

References cited on this page View Complete Literature Guide for JAC1
1) Strain J, et al.  (1998) Suppressors of superoxide dismutase (SOD1) deficiency in Saccharomyces cerevisiae. Identification of proteins predicted to mediate iron-sulfur cluster assembly. J Biol Chem 273(47):31138-44
2) Voisine C, et al.  (2001) Jac1, a mitochondrial J-type chaperone, is involved in the biogenesis of Fe/S clusters in Saccharomyces cerevisiae. Proc Natl Acad Sci U S A 98(4):1483-8
3) Kim R, et al.  (2001) J-domain protein, Jac1p, of yeast mitochondria required for iron homeostasis and activity of Fe-S cluster proteins. J Biol Chem 276(20):17524-32
4) Andrew AJ, et al.  (2006) Characterization of the interaction between the J-protein Jac1p and the scaffold for Fe-S cluster biogenesis, Isu1p. J Biol Chem 281(21):14580-7
5) Qiu XB, et al.  (2006) The diversity of the DnaJ/Hsp40 family, the crucial partners for Hsp70 chaperones. Cell Mol Life Sci 63(22):2560-2570
6) Cyr DM, et al.  (1994) DnaJ-like proteins: molecular chaperones and specific regulators of Hsp70. Trends Biochem Sci 19(4):176-81
7) Walsh P, et al.  (2004) The J-protein family: modulating protein assembly, disassembly and translocation. EMBO Rep 5(6):567-71