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J Biol Chem, Vol. 275, Issue 2, 1050-1056, January 14, 2000

Glycine Betaine-assisted Protein Folding in a lysA Mutant of Escherichia coli*

Stéphane BourotDagger , Olivier Sire§, Annie TrautwetterDagger , Thierry TouzéDagger , Long Fei Wu, Carlos BlancoDagger , and Théophile BernardDagger par

From the Dagger  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

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.

* 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.

par 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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