Structural Features of the GroEL-GroES Nano-Cage Required for Rapid Folding of Encapsulated Protein
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چکیده
منابع مشابه
Structural Features of the GroEL-GroES Nano-Cage Required for Rapid Folding of Encapsulated Protein
GroEL and GroES form a chaperonin nano-cage for proteins up to approximately 60 kDa to fold in isolation. Here we explored the structural features of the chaperonin cage critical for rapid folding of encapsulated substrates. Modulating the volume of the GroEL central cavity affected folding speed in accordance with confinement theory. Small proteins (approximately 30 kDa) folded more rapidly as...
متن کاملGroEL-GroES-mediated protein folding.
The chaperonin-mediated folding reaction is an essential ATP-dependent reaction that provides kinetic assistance to the process of protein folding to the native state in a variety of cellular compartments. This reaction, carried out by a megadalton-sized double ring “machine,” remains a fascination because it exhibits a multitude of interesting features, for example, allostery, with both positi...
متن کاملProtein unfolding and folding by GroEL-GroES
Background: Chaperonins like the GroEL-GroES complex facilitate protein folding in the cell. Results: Substrate proteins are captured by the open, trans ring of the GroEL-ATP-GroES complex and are partially unfolded. Conclusion: Maximally efficient folding requires repeated cycles of substrate protein unfolding by the GroEL-GroES complex. Significance: Establishing how substrate proteins are pr...
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The chaperonin GroEL binds nonnative proteins too large to fit inside the productive GroEL-GroES cis cavity, but whether and how it assists their folding has remained unanswered. We have examined yeast mitochondrial aconitase, an 82 kDa monomeric Fe(4)S(4) cluster-containing enzyme, observed to aggregate in chaperonin-deficient mitochondria. We observed that aconitase folding both in vivo and i...
متن کاملGroEL-GroES-mediated protein folding requires an intact central cavity.
The chaperonin GroEL is an oligomeric double ring structure that, together with the cochaperonin GroES, assists protein folding. Biochemical analyses indicate that folding occurs in a cis ternary complex in which substrate is sequestered within the GroEL central cavity underneath GroES. Recently, however, studies of GroEL "minichaperones" containing only the apical substrate binding subdomain h...
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ژورنال
عنوان ژورنال: Cell
سال: 2006
ISSN: 0092-8674
DOI: 10.1016/j.cell.2006.04.027