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Gene Review

YDJ1  -  type I HSP40 co-chaperone YDJ1

Saccharomyces cerevisiae S288c

Synonyms: HSP40, MAB3, MAS5, Mitochondrial protein import protein MAS5, N2418, ...
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Disease relevance of YDJ1

  • The 46-kDa protein YDJ1 is one of several known yeast homologues of the Escherichia coli DnaJ protein [1].
  • Hence, ZBDII is required for yeast to survive heat stress because it is essential for Ydj1 to cooperate with Hsp70 to suppress protein aggregation [2].
  • Mutations in genes encoding the molecular chaperones Hsp90 and Ydj1p suppress the toxicity of the protein tyrosine kinase p60v-src in yeast by reducing its levels or its kinase activity [3].

High impact information on YDJ1


Biological context of YDJ1

  • Haploid cells carrying the disrupted YDJ1 gene are inviable for growth in liquid media [6].
  • These results suggest that Ssa1p and Ydj1p chaperone activities play important roles in the regulation of microtubule formation in M phase [7].
  • In support of this idea, a ydj1 null mutant at the restrictive temperature was found to exhibit more prominent phenotypes than ssa1-134 [7].
  • The heat shock protein (Hsp) 70/Hsp40 chaperone system plays an essential role in cell physiology, but few of its in vivo functions are known [8].
  • Mutations in the yeast Hsp40 chaperone protein Ydj1 cause defects in Axl1 biogenesis and pro-a-factor processing [8].

Anatomical context of YDJ1


Associations of YDJ1 with chemical compounds

  • However, the Delta fes1 mutant showed increased cycloheximide sensitivity and a general translational defect, suggesting that Fes1p acts during protein translation, a process in which Ssa1p and Ydj1p are known to be involved [12].
  • In an otherwise wild-type background, the ydj1 mutation exerted strong and specific effects on three Hsp90 substrates, derepressing two (the estrogen and glucocorticoid receptors) and reducing the function of the third (the tyrosine kinase p60v-src) [5].
  • A role for the Hsp40 Ydj1 in repression of basal steroid receptor activity in yeast [13].
  • Glucocorticoid receptor containing a mutation in the carboxy-terminal transcriptional activation domain, AF-2, retained elevated basal activity, while mutation of the amino-terminal transactivation domain, AF-1, eliminated the elevated basal activity observed in ydj1 mutant strains [13].
  • A mutant form of YDJ1p, in which the conserved cysteine of the CaaX box is mutated to a serine (ydj1-S406p), cannot be farnesylated in vitro [14].

Regulatory relationships of YDJ1

  • In contrast, Ssa1p together with either of its Hsp40 cochaperones blocks Sup35p polymerization [15].
  • Collectively, these data indicate Ydj1p functions to promote AXL1 mRNA accumulation and in addition appears to facilitate the proper folding of nascent Axl1p [8].
  • The Hsp70-Ydj1 molecular chaperone represses the activity of the heme activator protein Hap1 in the absence of heme [16].
  • We observed that BiP, but not Ssa1p, is able to associate with GST-63Jp and that Ydj1p stimulates the ATPase activity of Ssa1p up to 10-fold but increases the ATPase activity of BiP by <2-fold [17].
  • The results suggest that Ydj1 inhibits Ure2 fibril formation by binding to the native state of Ure2, thus delaying the onset of oligomerization [18].

Other interactions of YDJ1

  • We further show that a related yeast protein, SIS1, is a multicopy suppressor of YDJ1 [6].
  • We show that Hsp104p greatly stimulates the assembly of Sup35p into fibrils, whereas Ydj1p has inhibitory effect [15].
  • In addition, a strain containing a single functional SSA gene, SSA1, and a deletion of YDJ1 accumulated the precursor form of alpha-factor [19].
  • First, AXL1 mRNA levels were reduced ydj1 strains [8].
  • We describe here our phenotypic analysis of two such mutants, hsf1-82 and ydj1-10, that affect the heat shock transcription factor and a yeast dnaj-like protein chaperone, respectively. hsf1-82 and ydj1-10 temperature-sensitive mutants arrest the cell division cycle at several stages [20].

Analytical, diagnostic and therapeutic context of YDJ1


  1. A conserved HPD sequence of the J-domain is necessary for YDJ1 stimulation of Hsp70 ATPase activity at a site distinct from substrate binding. Tsai, J., Douglas, M.G. J. Biol. Chem. (1996) [Pubmed]
  2. The type I Hsp40 zinc finger-like region is required for Hsp70 to capture non-native polypeptides from Ydj1. Fan, C.Y., Ren, H.Y., Lee, P., Caplan, A.J., Cyr, D.M. J. Biol. Chem. (2005) [Pubmed]
  3. CDC37 is required for p60v-src activity in yeast. Dey, B., Lightbody, J.J., Boschelli, F. Mol. Biol. Cell (1996) [Pubmed]
  4. YDJ1p facilitates polypeptide translocation across different intracellular membranes by a conserved mechanism. Caplan, A.J., Cyr, D.M., Douglas, M.G. Cell (1992) [Pubmed]
  5. Role of the protein chaperone YDJ1 in establishing Hsp90-mediated signal transduction pathways. Kimura, Y., Yahara, I., Lindquist, S. Science (1995) [Pubmed]
  6. Characterization of YDJ1: a yeast homologue of the bacterial dnaJ protein. Caplan, A.J., Douglas, M.G. J. Cell Biol. (1991) [Pubmed]
  7. Loss of Hsp70-Hsp40 chaperone activity causes abnormal nuclear distribution and aberrant microtubule formation in M-phase of Saccharomyces cerevisiae. Oka, M., Nakai, M., Endo, T., Lim, C.R., Kimata, Y., Kohno, K. J. Biol. Chem. (1998) [Pubmed]
  8. Mutations in the yeast Hsp40 chaperone protein Ydj1 cause defects in Axl1 biogenesis and pro-a-factor processing. Meacham, G.C., Browne, B.L., Zhang, W., Kellermayer, R., Bedwell, D.M., Cyr, D.M. J. Biol. Chem. (1999) [Pubmed]
  9. The glycine-phenylalanine-rich region determines the specificity of the yeast Hsp40 Sis1. Yan, W., Craig, E.A. Mol. Cell. Biol. (1999) [Pubmed]
  10. A yeast DnaJ homologue, Scj1p, can function in the endoplasmic reticulum with BiP/Kar2p via a conserved domain that specifies interactions with Hsp70s. Schlenstedt, G., Harris, S., Risse, B., Lill, R., Silver, P.A. J. Cell Biol. (1995) [Pubmed]
  11. The molecular chaperone Ydj1 is required for the p34CDC28-dependent phosphorylation of the cyclin Cln3 that signals its degradation. Yaglom, J.A., Goldberg, A.L., Finley, D., Sherman, M.Y. Mol. Cell. Biol. (1996) [Pubmed]
  12. Nucleotide exchange factor for the yeast Hsp70 molecular chaperone Ssa1p. Kabani, M., Beckerich, J.M., Brodsky, J.L. Mol. Cell. Biol. (2002) [Pubmed]
  13. A role for the Hsp40 Ydj1 in repression of basal steroid receptor activity in yeast. Johnson, J.L., Craig, E.A. Mol. Cell. Biol. (2000) [Pubmed]
  14. Farnesylation of YDJ1p is required for function at elevated growth temperatures in Saccharomyces cerevisiae. Caplan, A.J., Tsai, J., Casey, P.J., Douglas, M.G. J. Biol. Chem. (1992) [Pubmed]
  15. Molecular chaperones and the assembly of the prion Sup35p, an in vitro study. Krzewska, J., Melki, R. EMBO J. (2006) [Pubmed]
  16. The Hsp70-Ydj1 molecular chaperone represses the activity of the heme activator protein Hap1 in the absence of heme. Hon, T., Lee, H.C., Hach, A., Johnson, J.L., Craig, E.A., Erdjument-Bromage, H., Tempst, P., Zhang, L. Mol. Cell. Biol. (2001) [Pubmed]
  17. Specific molecular chaperone interactions and an ATP-dependent conformational change are required during posttranslational protein translocation into the yeast ER. McClellan, A.J., Endres, J.B., Vogel, J.P., Palazzi, D., Rose, M.D., Brodsky, J.L. Mol. Biol. Cell (1998) [Pubmed]
  18. Hsp40 interacts directly with the native state of the yeast prion protein Ure2 and inhibits formation of amyloid-like fibrils. Lian, H.Y., Zhang, H., Zhang, Z.R., Loovers, H.M., Jones, G.W., Rowling, P.J., Itzhaki, L.S., Zhou, J.M., Perrett, S. J. Biol. Chem. (2007) [Pubmed]
  19. Functional interaction of cytosolic hsp70 and a DnaJ-related protein, Ydj1p, in protein translocation in vivo. Becker, J., Walter, W., Yan, W., Craig, E.A. Mol. Cell. Biol. (1996) [Pubmed]
  20. A yeast heat shock transcription factor (Hsf1) mutant is defective in both Hsc82/Hsp82 synthesis and spindle pole body duplication. Zarzov, P., Boucherie, H., Mann, C. J. Cell. Sci. (1997) [Pubmed]
  21. Identification of Mrj, a DnaJ/Hsp40 family protein, as a keratin 8/18 filament regulatory protein. Izawa, I., Nishizawa, M., Ohtakara, K., Ohtsuka, K., Inada, H., Inagaki, M. J. Biol. Chem. (2000) [Pubmed]
  22. Purification, crystallization and preliminary X-ray crystallographic studies of S. cerevisiae Hsp40 Sis1. Sha, B., Cyr, D. Acta Crystallogr. D Biol. Crystallogr. (1999) [Pubmed]
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