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

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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