Chaperonin GroE and ADP facilitate the folding of various proteins and protect against heat inactivation.

Abstract:

:In the presence of ADP, the molecular chaperones GroEL and GroES from Escherichia coli not only facilitated the refolding of various proteins, but also prevented their irreversible heat inactivation in vitro. Without nucleotides the refolding reactions were arrested by GroEL. Addition of GroES and ADP to the reaction mixture initiated the refolding reactions and the enzyme activities were regained efficiently. The presence of GroE (GroEL and GroES) and ADP also protected against heat inactivation of native enzymes at various temperatures. These findings suggest that in the presence of GroES, nucleotide binding is an important event in the mechanism of GroEL-facilitated protein folding.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Kawata Y,Nosaka K,Hongo K,Mizobata T,Nagai J

doi

10.1016/0014-5793(94)00456-0

subject

Has Abstract

pub_date

1994-05-30 00:00:00

pages

229-32

issue

2-3

eissn

0014-5793

issn

1873-3468

pii

0014-5793(94)00456-0

journal_volume

345

pub_type

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