Roobol, A. and Sahyoun, Z.P. and Carden, M.J. (1999) Selected subunits of the cytosolic chaperonin associate with microtubules assembled in vitro. Journal of Biological Chemistry, 274 (4). pp. 2408-2415. ISSN 0021-9258.
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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 alpha, gamma, zeta, and theta also associated with in vitro assembled microtubules, i.e. behaved as microtubule-associated proteins. This nucleotide-dependent association between microtubules and CCT polypeptides (K-d similar to 0.1 mu M 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.
Q Science > QD Chemistry
Q Science > QH Natural history > QH301 Biology
|Divisions:||Faculties > Science Technology and Medical Studies > School of Biosciences|
|Depositing User:||F.D. Zabet|
|Date Deposited:||28 Mar 2009 23:14|
|Last Modified:||15 Apr 2009 11:20|
|Resource URI:||http://kar.kent.ac.uk/id/eprint/16567 (The current URI for this page, for reference purposes)|
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