Loading…

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 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 whi...

Full description

Saved in:
Bibliographic Details
Published in:Biochemical and biophysical research communications 1997-12, Vol.241 (3), p.687-692
Main Authors: Leroux, M.R, Candido, E.P.M
Format: Article
Language:English
Subjects:
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary: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.
ISSN:0006-291X
1090-2104
DOI:10.1006/bbrc.1997.7889