Functional characterisation of the chaperones DnaK, DnaJ, and GrpE from Clostridium acetobutylicum.

Abstract:

:The DnaK chaperone system is involved in various cellular processes such as the control of the folded and oligomeric state of proteins under stress and non-stress conditions. In this study we functionally characterised the homologues of the DnaK system from Clostridium acetobutylicum DnaK, DnaJ, GrpE and OrfA were heterologously synthesised in Escherichia coli and affinity purified via a His-tag. By optimising the stoichiometry, we were able to refold guanidinium hydrochloride-denatured firefly luciferase in vitro with 22% of the yield obtained with the E. coli DnaK system. In addition, C. acetobutylicum DnaJ could stimulate the E. coli DnaK ATPase by a factor of 55. Furthermore, the DnaK system from C. acetobutylicum was able to prevent the aggregation of OrfA from C. acetobutylicum, which is similar to the repressor HrcA of CIRCE-regulated heat shock genes in Bacillus subtilis.

journal_name

FEMS Microbiol Lett

authors

Rüngeling E,Laufen T,Bahl H

doi

10.1111/j.1574-6968.1999.tb13363.x

subject

Has Abstract

pub_date

1999-01-01 00:00:00

pages

119-23

issue

1

eissn

0378-1097

issn

1574-6968

pii

S0378-1097(98)00532-1

journal_volume

170

pub_type

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