Background information
The DnaJ family is one of the largest of all the chaperone families and has evolved with diverse cellular localization and functions. The presence of the J domain defines a protein as a member of the DnaJ family. DnaJ heat shock induced proteins are from the bacterium Escherichia coli and are under the control of the htpR regulatory protein. The DnaJ proteins play a critical role in the HSP 70 chaperone machine by interacting with HSP 70 to stimulate ATP hydrolysis. The proteins contain cysteine rich regions that are composed of zinc fingers that form a peptide-binding domain responsible for the chaperone function. DnaJ proteins are important mediators of proteolysis and are in-volved in the regulation of protein degradation, exocytsis and endocytosis. DnaJC7 (DnaJ homolog subfamily C member 7), also known as TPR2, TTC2 or DANJC7, is ubiquitously expressed, with highest expression in testis, liver, heart and brain.
