Hettema, E. H., Ruigrok, C. C. M., Koerkamp, M. G. et al. (4 more authors) (1998) The cytosolic DnaJ-like protein Djp1p is involved specifically in peroxisomal protein import. Journal of Cell Biology, 142 (2). pp. 421-434. ISSN 0021-9525
Abstract
The Saccharomyces cerevisiae DJP1 gene encodes a cytosolic protein homologous to Escherichia coli DnaJ. DnaJ homologues act in conjunction with molecular chaperones of the Hsp70 protein family in a variety of cellular processes. Cells with a DJP1 gene deletion are viable and exhibit a novel phenotype among cytosolic J-protein mutants in that they have a specific impairment of only one organelle, the peroxisome. The phenotype was also unique among peroxisome assembly mutants: peroxisomal matrix proteins were mislocalized to the cytoplasm to a varying extent, and peroxisomal structures failed to grow to full size and exhibited a broad range of buoyant densities. Import of marker proteins for the endoplasmic reticulum, nucleus, and mitochondria was normal. Furthermore, the metabolic adaptation to a change in carbon source, a complex multistep process, was unaffected in a DJP1 gene deletion mutant. We conclude that Djp1p is specifically required for peroxisomal protein import.
Metadata
Item Type: | Article |
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Authors/Creators: |
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Copyright, Publisher and Additional Information: | © 1998 Rockefeller University Press. CC BY-NC-SA |
Keywords: | molecular chaperone; peroxisome; DnaJ; import; Saccharomyces cerevisiae |
Dates: |
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Institution: | The University of Sheffield |
Academic Units: | The University of Sheffield > Faculty of Science (Sheffield) > School of Biosciences (Sheffield) > Department of Molecular Biology and Biotechnology (Sheffield) |
Depositing User: | Symplectic Sheffield |
Date Deposited: | 05 Dec 2016 14:38 |
Last Modified: | 05 Dec 2016 14:44 |
Published Version: | http://dx.doi.org/10.1083/jcb.142.2.421 |
Status: | Published |
Publisher: | Rockefeller University Press |
Refereed: | Yes |
Identification Number: | 10.1083/jcb.142.2.421 |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:108668 |