XDJ1, a gene encoding a novel non-essential DnaJ homologue from Saccharomyces cerevisiae

Schwarz, Elisabeth; Westermann, Benedikt; Caplan, Avrom J.; Ludwig, Gabriele; Neupert, Walter

doi:10.1016/0378-1119(94)90333-6

Cited by 19 publications

(11 citation statements)

References 16 publications

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“…It is known that Djp1 has a role in peroxisomal protein import, and it may be that this J protein is highly specialized for this role and no others 48 . Also, Xdj1 may not be expressed 49 .…”

Section: Resultsmentioning

confidence: 99%

Synthetic lethal interactions in yeast reveal functional roles of J protein co-chaperones

2012

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J proteins are a diverse family of co-chaperones that cooperate with heat shock protein 70 (Hsp70) to coordinate protein quality control, especially in response to cellular stress. Current models suggest that individual J proteins might play roles in recruiting Hsp70s to specific functions, such as maintaining cell wall integrity or promoting ribosome biogenesis. However, relatively few stresses have been used to test this model and, as a result, only a few specific activities have been identified. To expand our understanding of the J protein network, we used a synthetic lethal approach in which 11 Saccharomyces cerevisiae deletion strains were treated with 12 well-characterized chemical inhibitors. The results defined new roles for specific J proteins in major signaling pathways. For example, an important role for Swa2 in cell wall integrity was identified and activities of the under-explored Jjj1, Apj1, Jjj3 and Caj1 proteins were suggested. More generally, these findings support a model in which some J proteins, such as Ydj1 and Zuo1, play “generalist” roles, while others, such as Apj1 and Jjj2, are “specialists”, having roles in relatively few pathways. Together, these results provide new insight into the network of J proteins.

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Section: Resultsmentioning

confidence: 99%

Synthetic lethal interactions in yeast reveal functional roles of J protein co-chaperones

2012

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“…In other cases, we also found ER or mitochondrial chaperones interacting with cytoplasmic proteins. This might reflect the multiple localization of the protein or chaperone; for example, Xdj1 has been reported to be a mitochondrial as well as a cytoplasmic protein (Figure 1) (Schwarz et al , 1994; Reinders et al , 2006; Sahi and Craig, 2007). Alternatively, the detected interaction might be a false positive hit, possibly occurring post‐lysis.…”

Section: Discussionmentioning

confidence: 99%

An atlas of chaperone–protein interactions in Saccharomyces cerevisiae : implications to protein folding pathways in the cell

Gong

Kakihara

Krogan

et al. 2009

Molecular Systems Biology

218

277

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Molecular chaperones are known to be involved in many cellular functions, however, a detailed and comprehensive overview of the interactions between chaperones and their cofactors and substrates is still absent. Systematic analysis of physical TAP-tag based protein-protein interactions of all known 63 chaperones in Saccharomyces cerevisiae has been carried out. These chaperones include seven small heat-shock proteins, three members of the AAA þ family, eight members of the CCT/TRiC complex, six members of the prefoldin/GimC complex, 22 Hsp40s, 1 Hsp60, 14 Hsp70s, and 2 Hsp90s. Our analysis provides a clear distinction between chaperones that are functionally promiscuous and chaperones that are functionally specific. We found that a given protein can interact with up to 25 different chaperones during its lifetime in the cell. The number of interacting chaperones was found to increase with the average number of hydrophobic stretches of length between one and five in a given protein. Importantly, cellular hot spots of chaperone interactions are elucidated. Our data suggest the presence of endogenous multicomponent chaperone modules in the cell.

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“…The DnaJ family is present in many species, from E. coli to human. There are six related sequences in yeast (Sadler et al, 1989;Blumberg and Silver, 1991;Caplan and Douglas, 1991;Luke er al., 1991;Atencio and Yaffe, 1992;Zhang et aE., 1992;Rowley et al, 1994;Schwarz et al, 1994).…”

Section: Yib4w) Expands the Dnaj Familymentioning

confidence: 99%

Nucleotide sequence and analysis of the centromeric region of yeast chromosome IX

Voß¹,

Tamames²,

Teodoru³

et al. 1995

Yeast

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We have determined the nucleotide sequence of a cosmid (pIX338) containing the centromere region of yeast (Saccharomyces cerevisiae) chromosome IX. The complete nucleotide sequence of 33.8 kb was obtained by using an efficient directed sequencing strategy in combination with automated DNA sequencing on the A.L.F. DNA sequencer. Sequence analysis revealed the presence of 17 open reading frames (ORFs), four of them previously known yeast genes (sly12, pan1, sts1 and prl1), a tRNA gene and the centromere motif. Exhaustive database searches detected sequence homologues of known function for as many as 14 of the 17 ORFs. These include a mammalian tyrosine kinase substrate; the Escherichia coli cell cycle protein MinD; the human inositol polyphosphate-5-phosphatase (gene OCRL) involved in Lowe's syndrome, a developmental disorder; and helicases, for which the new yeast member defines a distinct DEAD/H-box subfamily. A surprisingly large fraction of the ORFs (at least six out of 17) in the centromeric region are apparently involved in RNA or DNA binding.

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XDJ1, a gene encoding a novel non-essential DnaJ homologue from Saccharomyces cerevisiae

Cited by 19 publications

References 16 publications

Synthetic lethal interactions in yeast reveal functional roles of J protein co-chaperones

Synthetic lethal interactions in yeast reveal functional roles of J protein co-chaperones

An atlas of chaperone–protein interactions in Saccharomyces cerevisiae : implications to protein folding pathways in the cell

Nucleotide sequence and analysis of the centromeric region of yeast chromosome IX

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