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J. Biol. Chem., Vol. 269, Issue 4, 2447-2451, Jan, 1994
JA Mendoza, B Demeler and PM Horowitz
Chaperonin-mediated, in vitro folding of rhodanese by the intact protein
cpn60 has previously been shown to require cpn10 and ATP hydrolysis
(Martin, J., Langer, T., Boteva, R., Schramel, A., Horwich, A. L., and
Hartl, F.-U. (1991) Nature 352, 36-42; Mendoza, J. A., Rogers, E., Lorimer,
G. H., and Horowitz, P. M. (1991) J. Biol. Chem. 266, 13044-13049). The
present work demonstrates that the rhodanese- cpn60 complex can be
dissociated by urea to allow folding to proceed, thus removing the
obligatory requirement for cpn10 and ATP. Analytical ultracentrifugation
and circular dichroism show that tetradecameric cpn60 can be disassembled
into monomers that retain substantial secondary structure. Unfolded
rhodanese induces the reassembly of tetradecameric cpn60 from monomers, and
binding of rhodanese stabilizes cpn60 quaternary structure. Intermediate
cpn60 species, possibly heptamers, are detected at intermediate urea
concentrations after addition of unfolded rhodanese. The use of urea has
demonstrated a functionally related loosening of subunit interactions in
cpn60 that is not detectable under usual solution conditions. Our data
suggest a highly dynamic role for the quaternary structure of cpn60 in
chaperonin- mediated protein folding.
Alteration of the quaternary structure of cpn60 modulates chaperonin- assisted folding. Implications for the mechanism of chaperonin action
Department of Biochemistry, University of Texas Health Science Center, San Antonio 78240-7760.
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