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A homologue of the bacterial heat-shock gene DnaJ that alters protein sorting in yeast

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Abstract

HEAT-shock proteins have been implicated in assembly of protein complexes1, correct protein folding2 and uptake of proteins into organdies3–4. In Escherichia coli, the heat-shock protein DnaJ and the HspTO homologue, DnaK, act together to disassemble a protein complex involved in bacteriophage λ replication5. We report the identification of SCJ1, a gene in the yeast Saccharomyces cerevisiae that encodes a homologue of the bacterial DnaJ protein. SCJ1 was identified by a genetic screen in which increased expression of candidate genes results in missorting of a nuclear-targeted test protein. The predicted amino-acid sequence of SCJ1 is 37% identical to the entire E. coli DnaJ protein. Hybridization experiments indicate that there is a family of yeast genes related to SCJ1. These findings suggest that the HspTO DnaK-DnaJ interaction is general to eukaryotes.

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  1. Department of Molecular Biology, Princeton University, Princeton, New Jersey, 08544, USA

    Hal Blumberg & Pamela A. Silver

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  1. Hal Blumberg
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  2. Pamela A. Silver
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Blumberg, H., Silver, P. A homologue of the bacterial heat-shock gene DnaJ that alters protein sorting in yeast. Nature 349, 627–630 (1991). https://doi.org/10.1038/349627a0

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