YDJ1/YNL064C Summary Help

Standard Name YDJ1 1
Systematic Name YNL064C
Alias MAS5 2 , HSP40 , MAB3 3
Feature Type ORF, Verified
Description Type I HSP40 co-chaperone; involved in regulation of HSP90 and HSP70 functions; critical for determining cell size at Start as a function of growth rate; involved in protein translocation across membranes; member of the DnaJ family (1, 4, 5, 6, 7, 8, 9 and see Summary Paragraph)
Name Description Yeast dnaJ 1
Chromosomal Location
ChrXIV:507097 to 505868 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
Gbrowse
Gene Ontology Annotations All YDJ1 GO evidence and references
  View Computational GO annotations for YDJ1
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
Regulators 7 genes
Resources
Classical genetics
conditional
null
overexpression
unspecified
Large-scale survey
null
overexpression
unspecified
Resources
623 total interaction(s) for 483 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 51
  • Affinity Capture-RNA: 6
  • Affinity Capture-Western: 17
  • Biochemical Activity: 7
  • Co-crystal Structure: 2
  • Co-fractionation: 1
  • Co-purification: 3
  • PCA: 1
  • Reconstituted Complex: 7
  • Two-hybrid: 1

Genetic Interactions
  • Dosage Growth Defect: 2
  • Dosage Rescue: 17
  • Negative Genetic: 342
  • Phenotypic Enhancement: 5
  • Phenotypic Suppression: 3
  • Positive Genetic: 102
  • Synthetic Growth Defect: 16
  • Synthetic Lethality: 38
  • Synthetic Rescue: 2

Resources
Expression Summary
histogram
Resources
Length (a.a.) 409
Molecular Weight (Da) 44,670
Isoelectric Point (pI) 6.23
Localization
Phosphorylation PhosphoGRID | PhosphoPep Database
Structure
Homologs
sequence information
ChrXIV:507097 to 505868 | 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..1230 507097..505868 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 SGDIDS000005008
SUMMARY PARAGRAPH for YDJ1

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 10, 11, and 12). 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 12). 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 (12).

Ydj1p is the regulating partner for the cytosolic Hsp70s Ssa1p and Ssa2p (and presumably the paralogs Ssa3p and Ssa4p) (13, 14). As an Ssa co-chaperone, Ydj1p is involved in the processes of cellular stress response, protein folding and re-folding (15, 16), suppression and rescue of protein aggregates (17, 18), mitochondrial and ER protein translocation (1, 6), establishment of Hsp90-mediated signal transduction pathways (4), and ubquitin-dependent degradation (19).

Loss of Ydj1p function results in defective mating, alpha-factor secretion, and inability to properly fold a heterologously expressed human androgen receptor protein (20, 21). Null mutations in ydj1 lead to a slow growth phenotype at 25 degrees C on solid media, and lethality in cells grown at 37 degrees C or in liquid culture (21, 1). This temperature-sensitive phenotype can be complemented by heterologous expression of either plant ANJ1, trypanosome TCJ2, or rat RDJ1 (22, 23, 24). YDJ1 overexpression has been studied in yeast models of human prion disease such as Creutzfeldt-Jakob disease (OMIM) and has been found to cure cells propagating the [PSI+] and [URE3] prions (isoforms of Sup35p and Ure2p, respectively) (25, 26, 27).

Comparative, mutational, and crystal structure analyses show that Ydj1p contains all of the structurally defined domains found in bacterial DnaJ, human Hdj2 (OMIM) and other type I Hsp40 proteins: an amino-terminal J domain linked by a glycine and phenylalanine-rich region to a zinc finger-like region (ZFLR) followed by a conserved carboxyl-terminal domain (1, 16, 21, 28, 12). Like other type I and type II Hsp40s, Ydj1p functions as a homodimer with protein dimerization being mediated by the Ydj1p C-terminus (29). The Ydj1p ZFLR has been shown to be required for substrate transfer to Hsp70 (21). Ydj1p is also a target for farnesylation, a modification that is necessary for the protein to function at elevated temperatures (30).

Last updated: 2006-12-19 Contact SGD

References cited on this page View Complete Literature Guide for YDJ1
1) Caplan AJ and Douglas MG  (1991) Characterization of YDJ1: a yeast homologue of the bacterial dnaJ protein. J Cell Biol 114(4):609-21
2) Atencio DP and Yaffe MP  (1992) MAS5, a yeast homolog of DnaJ involved in mitochondrial protein import. Mol Cell Biol 12(1):283-91
3) Tomita Y, et al.  (2003) Mutation of host DnaJ homolog inhibits brome mosaic virus negative-strand RNA synthesis. J Virol 77(5):2990-7
4) Kimura Y, et al.  (1995) Role of the protein chaperone YDJ1 in establishing Hsp90-mediated signal transduction pathways. Science 268(5215):1362-5
5) Ziegelhoffer T, et al.  (1995) The dissociation of ATP from hsp70 of Saccharomyces cerevisiae is stimulated by both Ydj1p and peptide substrates. J Biol Chem 270(18):10412-9
6) Caplan AJ, et al.  (1992) YDJ1p facilitates polypeptide translocation across different intracellular membranes by a conserved mechanism. Cell 71(7):1143-55
7) Hon T, et al.  (2001) The Hsp70-Ydj1 molecular chaperone represses the activity of the heme activator protein Hap1 in the absence of heme. Mol Cell Biol 21(23):7923-32
8) Summers DW, et al.  (2009) Prion propagation by Hsp40 molecular chaperones. Prion 3(2):59-64
9) Ferrezuelo F, et al.  (2012) The critical size is set at a single-cell level by growth rate to attain homeostasis and adaptation. Nat Commun 3():1012
10) 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
11) Cyr DM, et al.  (1994) DnaJ-like proteins: molecular chaperones and specific regulators of Hsp70. Trends Biochem Sci 19(4):176-81
12) Walsh P, et al.  (2004) The J-protein family: modulating protein assembly, disassembly and translocation. EMBO Rep 5(6):567-71
13) Cyr DM, et al.  (1992) Regulation of Hsp70 function by a eukaryotic DnaJ homolog. J Biol Chem 267(29):20927-31
14) Cyr DM and Douglas MG  (1994) Differential regulation of Hsp70 subfamilies by the eukaryotic DnaJ homologue YDJ1. J Biol Chem 269(13):9798-804
15) Lu Z and Cyr DM  (1998) The conserved carboxyl terminus and zinc finger-like domain of the co-chaperone Ydj1 assist Hsp70 in protein folding. J Biol Chem 273(10):5970-8
16) Tsai J and Douglas MG  (1996) A conserved HPD sequence of the J-domain is necessary for YDJ1 stimulation of Hsp70 ATPase activity at a site distinct from substrate binding. J Biol Chem 271(16):9347-54
17) Cyr DM  (1995) Cooperation of the molecular chaperone Ydj1 with specific Hsp70 homologs to suppress protein aggregation. FEBS Lett 359(2-3):129-32
18) Glover JR and Lindquist S  (1998) Hsp104, Hsp70, and Hsp40: a novel chaperone system that rescues previously aggregated proteins. Cell 94(1):73-82
19) Lee DH, et al.  (1996) Involvement of the molecular chaperone Ydj1 in the ubiquitin-dependent degradation of short-lived and abnormal proteins in Saccharomyces cerevisiae. Mol Cell Biol 16(9):4773-81
20) Meacham GC, et al.  (1999) Mutations in the yeast Hsp40 chaperone protein Ydj1 cause defects in Axl1 biogenesis and pro-a-factor processing. J Biol Chem 274(48):34396-402
21) Fan CY, et al.  (2005) The type I Hsp40 zinc finger-like region is required for Hsp70 to capture non-native polypeptides from Ydj1. J Biol Chem 280(1):695-702
22) Zhu JK, et al.  (1993) Isoprenylation of the plant molecular chaperone ANJ1 facilitates membrane association and function at high temperature. Proc Natl Acad Sci U S A 90(18):8557-61
23) Edkins AL, et al.  (2004) A Trypanosoma cruzi heat shock protein 40 is able to stimulate the adenosine triphosphate hydrolysis activity of heat shock protein 70 and can substitute for a yeast heat shock protein 40. Int J Biochem Cell Biol 36(8):1585-98
24) Leng CH, et al.  (1998) Isolation and characterization of a DnaJ-like protein in rats: the C-terminal 10-kDa domain of hsc70 is not essential for stimulating the ATP-hydrolytic activity of hsc70 by a DnaJ-like protein. Protein Sci 7(5):1186-94
25) Kryndushkin DS, et al.  (2002) Increased expression of Hsp40 chaperones, transcriptional factors, and ribosomal protein Rpp0 can cure yeast prions. J Biol Chem 277(26):23702-8
26) Krzewska J and Melki R  (2006) Molecular chaperones and the assembly of the prion Sup35p, an in vitro study. EMBO J 25(4):822-33
27) Moriyama H, et al.  (2000) [URE3] prion propagation in Saccharomyces cerevisiae: requirement for chaperone Hsp104 and curing by overexpressed chaperone Ydj1p. Mol Cell Biol 20(23):8916-22
28) Li J, et al.  (2003) The crystal structure of the yeast Hsp40 Ydj1 complexed with its peptide substrate. Structure 11(12):1475-83
29) Wu Y, et al.  (2005) The crystal structure of the C-terminal fragment of yeast Hsp40 Ydj1 reveals novel dimerization motif for Hsp40. J Mol Biol 346(4):1005-11
30) Caplan AJ, et al.  (1992) Farnesylation of YDJ1p is required for function at elevated growth temperatures in Saccharomyces cerevisiae. J Biol Chem 267(26):18890-5