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J Biol Chem, Vol. 274, Issue 4, 2408-2415, January 22, 1999
From the Department of Biosciences, University of Kent, Canterbury,
Kent CT2 7NJ, United Kingdom
The molecular chaperone activities of the only
known chaperonin in the eukaryotic cytosol (cytosolic chaperonin
containing T-complex polypeptide 1 (CCT)) appear to be relatively
specialized; the main folding substrates in vivo and
in vitro are identified as tubulins and actins. CCT is
unique among chaperonins in the complexity of its hetero-oligomeric
structure, containing eight different, although related, gene products.
In addition to their known ability to bind to and promote correct
folding of newly synthesized and denatured tubulins, we show here that
CCT subunits
Selected Subunits of the Cytosolic Chaperonin Associate with
Microtubules Assembled in Vitro
, 
, 
, and 
also associated with in
vitro assembled microtubules, i.e. behaved as
microtubule-associated proteins. This nucleotide-dependent association between microtubules and CCT polypeptides
(Kd ~ 0.1 µM CCT subunit) did not
appear to involve whole oligomeric chaperonin particles, but rather
free CCT subunits. Removal of the tubulin COOH termini by subtilisin
digestion caused all eight CCT subunits to associate with the
microtubule polymer, thus highlighting the non-chaperonin nature of the
selective CCT subunit association with normal microtubules.
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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