Roles of molecular chaperones in cytoplasmic protein folding.

Abstract:

:Newly synthesized polypeptide chains must fold and assemble into unique three-dimensional structures in order to become functionally active. In many cases productive folding depends on assistance from molecular chaperones, which act in preventing off-pathway reactions during folding that lead to aggregation. The inherent tendency of incompletely folded polypeptide chains to aggregate is thought to be strongly enhanced$L in vivo *I$Lby the high macromolecular concentration of the cellular solution, resulting in crowding effects, and by the close proximity of nascent polypeptide chains during synthesis on polyribosomes. The major classes of chaperones acting in cytoplasmic protein folding are the Hsp70s and the chaperonins. Hsp70 chaperones shield the hydrophobic regions of nascent and incompletely folded chains, whereas the chaperonins provide a sequestered environment in which folding can proceed unimpaired by intermolecular interactions between non-native polypeptides. These two principles of chaperone action can function in a coordinated manner to ensure the efficient folding of a subset of cytoplasmic proteins.

journal_name

Semin Cell Dev Biol

authors

Agashe VR,Hartl FU

doi

10.1006/scdb.1999.0347

subject

Has Abstract

pub_date

2000-02-01 00:00:00

pages

15-25

issue

1

eissn

1084-9521

issn

1096-3634

pii

S1084-9521(99)90347-6

journal_volume

11

pub_type

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