The folding of proteins and the assembly of protein complexes within s
ubcompartments of the eukaryotic cell is catalysed by different member
s of the Hsp70 protein family. The chaperone function of Hsp70 protein
s in these events is regulated by members of the DnaJ-like protein fam
ily, which occurs through direct interaction of different Hsp70 and Dn
aJ-like protein pairs that appear to be specifically adapted to each o
ther. This review highlights the diversity of functions of DnaJ-like p
roteins by using specific examples of DnaJ-Hsp70 interactions with pol
ypeptides in yeast protein-biogenesis pathways.