منابع مشابه
GroEL-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 کاملStructure and function in GroEL-mediated protein folding.
Recent structural and biochemical investigations have come together to allow a better understanding of the mechanism of chaperonin (GroEL, Hsp60)-mediated protein folding, the final step in the accurate expression of genetic information. Major, asymmetric conformational changes in the GroEL double toroid accompany binding of ATP and the cochaperonin GroES. When a nonnative polypeptide, bound to...
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...
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...
متن کاملGroEL/GroES-Mediated Folding of a Protein Too Large to Be Encapsulated
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...
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ژورنال
عنوان ژورنال: Protein Science
سال: 1997
ISSN: 0961-8368
DOI: 10.1002/pro.5560060401