A 68-kDa heat-stress protein (HSP68) has been purified from cell-suspe
nsion cultures of tomato (Lycopersicon peruvianum L.). Antibodies rais
ed against HSP68 cross-react with the Escherichia coli heat-stress pro
tein DnaK. HSP68 was found to be a hydrophilic, ATP-binding protein. I
mmunological analysis of subcellular fractions and immunogold-labellin
g of ultrathin sections showed consistently that HSP68 is localized in
the mitochondrial matrix. In-vitro translation experiments indicated
that HSP68 is synthesized as a precursor protein. Immunoscreening of c
DNA libraries from tomato and potato (Solanum tuberosum L.) led to the
isolation of corresponding cDNA clones. The deduced amino-acid sequen
ces show strong relationships to the DnaK-like proteins from bacteria
and organelles of eukaryotic cells. The protein HSP68 is constitutivel
y expressed, but its synthesis is increased during heat stress in all
cells of higher plantes investigated so far.