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

Biochemical and Biophysical Research Communications
Michel R Leroux, E P Candido

Abstract

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.

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Oct 31, 2008·BMC Bioinformatics·Matthew T WeirauchJoshua M Stuart
Jan 1, 2014·Frontiers in Molecular Biosciences·Anna FrumkinAnat Ben-Zvi
Apr 5, 2008·Developmental Dynamics : an Official Publication of the American Association of Anatomists·Surajit Sarkar, S C Lakhotia
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