In vitro dissociation of self-assembly of three chaperonin 60s: the role of ATP.

Abstract:

:A comparative study has investigated the in vitro dissociation and self-assembly of chaperonin 60 14-mers isolated from E. coli (GroEL), yeast mitochondria and pea chloroplasts. In all cases Mg2+ inhibits, and low temperature stimulates, the urea-induced dissociation. ATP or ADP in the presence of Mg2+ enhance the dissociation of the chaperonins. Re-assembly of the 14-mers from their monomers shows different efficiencies between the three proteins. In all cases, however, self-assembly is stimulated by Mg-adenine nucleotides. Surprisingly, effective self-assembly of GroEL is promoted by 20% glycerol in the absence of ATP. The role of Mg-adenine nucleotides in the dissociation and assembly of the chaperonins is discussed.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Lissin NM

doi

10.1016/0014-5793(95)00151-x

subject

Has Abstract

pub_date

1995-03-13 00:00:00

pages

55-60

issue

1

eissn

0014-5793

issn

1873-3468

pii

001457939500151X

journal_volume

361

pub_type

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