Chaperonin facilitates protein folding by avoiding polypeptide collapse
نویسندگان
چکیده
1 Department of Molecular Bioscience, Kyoto Sangyo University, Kamigamo-Motoyama, Kyoto, 603-8555, Japan, 2 present address: Biotechnology Research Center and Department of Biotechnology, Toyama Prefectural University, 5180 Kurokawa, Imizu, Toyama 939-0398, Japan; Asano Active Enzyme Molecule Project, ERATO, JST, 5180 Kurokawa, Imizu, Toyama 939-0398, Japan; 4 present address: Daiichi Yakuhin Kogyo Co.,Ltd., Kusashima 15-1, Toyama, Toyama 930-2201, Japan
منابع مشابه
The effect of macromolecular crowding on chaperonin-mediated protein folding.
The cylindrical chaperonin GroEL and its cofactor GroES mediate ATP-dependent protein folding in Escherichia coli. Recent studies in vitro demonstrated that GroES binding to GroEL causes the displacement of unfolded polypeptide into the central volume of the GroEL cavity for folding in a sequestrated environment. Resulting native protein leaves GroEL upon GroES release, whereas incompletely fol...
متن کاملChaperonin-mediated protein folding: fate of substrate polypeptide.
Chaperonins are megadalton ring assemblies that mediate essential ATP-dependent assistance of protein folding to the native state in a variety of cellular compartments, including the mitochondrial matrix, the eukaryotic cytosol, and the bacterial cytoplasm. Structural studies of the bacterial chaperonin, GroEL, both alone and in complex with its co-chaperonin, GroES, have resolved the states of...
متن کاملPolypeptide in the chaperonin cage partly protrudes out and then folds inside or escapes outside.
The current mechanistic model of chaperonin-assisted protein folding assumes that the substrate protein in the cage, formed by GroEL central cavity capped with GroES, is isolated from outside and exists as a free polypeptide. However, using ATPase-deficient GroEL mutants that keep GroES bound, we found that, in the rate-limiting intermediate of a chaperonin reaction, the unfolded polypeptide in...
متن کاملMonitoring Protein Conformation along the Pathway of Chaperonin-Assisted Folding
The GroEL/GroES chaperonin system mediates protein folding in the bacterial cytosol. Newly synthesized proteins reach GroEL via transfer from upstream chaperones such as DnaK/DnaJ (Hsp70). Here we employed single molecule and ensemble FRET to monitor the conformational transitions of a model substrate as it proceeds along this chaperone pathway. We find that DnaK/DnaJ stabilizes the protein in ...
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 کامل