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J Biol Chem, Vol. 275, Issue 2, 1050-1056, January 14, 2000
From the Osmoprotectants exogenously supplied to a
hyperosmotic culture medium are efficiently imported and amassed by
stressed cells of Escherichia coli. In addition to their
evident role in the recovery and maintenance of osmotic balance, these
solutes should play an important role on the behavior of cellular
macromolecules, for example in the process of protein folding. Using a
random chemical mutagenesis approach, a conditional lysine auxotrophic mutant was obtained. The growth of this mutant was restored by addition
of either lysine or osmoprotectants including glycine betaine (GB) in
the minimal medium. The growth rate increased proportionally with the
augmentation of the intracellular GB concentration. The mutation was
located in the lysA gene and resulted in the substitution
of the Ser at position 384 by Phe of the diaminopimelate decarboxylase
(DAPDC), which catalyzes the conversion of
meso-diaminopimelate to L-lysine. We purified
both the wild type DAPDC and the mutated DAPDC-sf and demonstrated that
GB was capable of activating DAPDC-sf in vitro, thus
confirming the in vivo results. Most importantly, we showed
that the activation was correlated with a conformational change of
DAPDC-sf. Taken together, these results show, for the first time, that
GB may actively assist in vivo protein folding in a
chaperone-like manner.
Glycine Betaine-assisted Protein Folding in a lysA
Mutant of Escherichia coli*
,,,, and
Groupe Membranes et Osmorégulation,
CNRS UPRES-A 6026, Université de Rennes I, Campus de Beaulieu,
35042 Rennes, France, § Laboratoire de Biologie et Chimie
Moléculaires, Université de Bretagne-Sud, 12 avenue St
Symphorien, 56017 Vannes, France, and the ¶ Laboratoire de Chimie
Bactérienne, UPR 9043 CNRS, Institut de Biologie Structurale
et Microbiologie, 31 chemin Joseph Aiguier,
13402 Marseille, France
*
This work was supported by grants from the Centre National
de la Recherche Scientifique and the Direction de la Recherche et des
Etudes Doctorales.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed: Groupe Membranes
et Osmorégulation, CNRS UPRES-A 6026, Bâtiment 14, Campus
de Beaulieu, 35042 Rennes cedex, France. Tel.: 33-299-28-61-41; Fax: 33-299-28-61-40; E-mail: tbernard@univ-rennes1.fr.
Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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