SUBUNIT CHARACTERIZATION OF THE CAENORHABDITIS-ELEGANS CHAPERONIN CONTAINING TCP-1 AND EXPRESSION PATTERN OF THE GENE ENCODING CCT-1

The chaperonin containing TCP-1 (CCT) from the free-living nematode Ca enorhabditis elegans was purified and shown to contain at least seven subunit species ranging from 52-65 kDa. SDS gel electrophoresis and We stern 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 simi lar. Surprisingly, the co-purified HSP60 chaperonin present in the C. elegans CCT preparation has the greatest binding activity for denature d actin. Expression of a reporter gene under the control of the C. ele gans cct-1 promoter is found to be mainly restricted to neuronal and m uscle tissues, an observation which is consistent with the participati on of CCT in actin and tubulin folding. (C) 1997 Academic Press.