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Chaperonins: The hunt for the Group II mechanism.

Abstract：

:Chaperonins are multi-subunit complexes that enhance the efficiency of protein-folding reactions by capturing protein substrates in their central cavities. They occur in all prokaryotic and eukaryotic cell types and, alone amongst molecular chaperones, chaperonin knockouts are always lethal. Chaperonins come in two forms; the Group I are found in bacteria, mitochondria and plastids [W.A. Fenton, A.L. Horwich, Q. Rev. Biophys. 36 (2003) 229-256, [1]] and the Group II in the eukaryotic cytoplasm and in archaea [N.J. Cowan, S.A. Lewis, Adv. Protein Chem. 59 (2001) 73-104, [2]]. Both use energy derived from ATP binding and hydrolysis to drive a series of structural rearrangements that enable them to capture, engulf and then release polypeptide chains that have either not yet acquired the native, biologically active state or have been denatured in the cell.

journal_name

Arch Biochem Biophys

journal_title

Archives of biochemistry and biophysics

authors

Bigotti MG,Clarke AR

doi

10.1016/j.abb.2008.03.015

subject

Has Abstract

pub_date

2008-06-15 00:00:00

pages

331-9

issue

2

eissn

0003-9861

issn

1096-0384

pii

S0003-9861(08)00157-4

journal_volume

474

pub_type

杂志文章,评审

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