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Originally published In Press as doi:10.1074/jbc.M102098200 on June 6, 2001

J. Biol. Chem., Vol. 276, Issue 32, 29906-29914, August 10, 2001
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Characterization of a Novel Complex from Halophilic Archaebacteria, Which Displays Chaperone-like Activities in Vitro*

Bruno FranzettiDagger §, Guy Schoehn, Christine EbelDagger , Jean Gagnon||, Rob W. H. Ruigrok, and Giuseppe ZaccaiDagger

From the Dagger  Laboratoire de Biophysique Moléculaire and || Laboratoire d'Enzymologie Moléculaire Institute of Structural Biology, CNRS-Commisariat à l'Energie Atomique-Université Joseph Fourier, 41 rue J. Horowitz, 38027 Grenoble Cedex 1, and the  EMBL Grenoble Outstation, EMBL, PB181, 38042 Grenoble Cedex 9, France

We isolated a protein, P45, from the extreme halophilic archaeon Haloarcula marismortui, which displays molecular chaperone activities in vitro. P45 is a weak ATPase that assembles into a large ring-shaped oligomeric complex comprising about 10 subunits. The protein shows no significant homology to any known protein. P45 forms complexes with halophilic malate dehydrogenase during its salt-dependent denaturation/renaturation and decreases the rate of deactivation of the enzyme in an ATP-dependent manner. Compared with other halophilic proteins, the P45 complex appears to be much less dependent on salt for its various activities or stability. In vivo experiments showed that P45 accumulates when cells are exposed to a low salt environment. We suggest, therefore, that P45 could protect halophilic proteins against denaturation under conditions of cellular hyposaline stress.

* 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: Institut de Biologie Structurale, CNRS/CEA, 41 rue J. Horowitz, 38027 Grenoble Cedex 1, France. Tel.: 33-476-88-9569; Fax: 33-476-88-5494. E-mail: franzetti@ibs.fr.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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