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J. Cell Biol.,
Volume 142, Number 2, July 27, 1998 421-434
Department of Biochemistry, Academic Medical Center, 1105 AZ Amsterdam, The Netherlands
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.
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