Subunit characterization of the Caenorhabditis elegans chaperonin containing TCP-1 and expression pattern of the gene...

The chaperonin containing TCP-1 (CCT) from the free-living nematode Caenorhabditis elegans was purified and shown to contain at least seven subunit species ranging from 52-65 kDa. SDS-gel electrophoresis and Western blot analyses with antibodies against C. elegans CCT-1 and CCT-5 and an antibody which recognizes a conserved region in vertebrate CCT subunits confirm that the subunit compositions of CCTs from distantly related organisms (C. elegans and bovine species) are remarkably similar. Surprisingly, the co-purified HSP60 chaperonin present in the C. elegans CCT preparation has the greatest binding activity for denatured actin. Expression of a reporter gene under the control of the C. elegans cct-1 promoter is found to be mainly restricted to neuronal and muscle tissues, an observation which is consistent with the participation of CCT in actin and tubulin folding.