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Published online before print April 9, 2004, 10.1110/ps.03566004
Protein Science (2004), 13:1295-1303. Published by Cold Spring Harbor Laboratory Press. Copyright © 2004 The Protein Society
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Deciphering the function of an ORF: Salmonella enterica DeoM protein is a new mutarotase specific for deoxyribose

Liliane Assairi1,6, Thomas Bertrand3,8, Joëlle Ferdinand1, Neli Slavova-Azmanova1, Mette Christensen4, Pierre Briozzo5, Francis Schaeffer2, Constantin T. Craescu6, Jan Neuhard4, Octavian Bârzu1 and Anne-Marie Gilles1,7

1 Laboratoire de Chimie Structurale des Macromolécules and
2 Unité de Biochimie Structurale, Unité de Recherche Associeé (URA) 2185 du Centre National de la Recherche Scientifique (CNRS), Institut Pasteur, 75724 Paris Cedex 15, France
3 Laboratoire d’ Enzymologie et Biochimie Structurale, Unité Propre du Recherche (UPR) 9063 du CNRS, 91198 Gif sur Yvette Cedex, France
4 Department of Biological Chemistry, Institute of Molecular Biology, University of Copenhagen, Copenhagen K, Denmark
5 Laboratoire de Chimie Biologique, Institut National Agronomique Paris-Grignon, 78850 Thiverval-Grignon, France
6 Institut National de la Santé et de la Recherche Médicale U350 and Institut Curie, Centre Universitaire Paris-Sud, 91405 Orsay, France

(RECEIVED December 15, 2003; FINAL REVISION January 29, 2004; ACCEPTED January 29, 2004)



Abstract

We identified in Salmonella enterica serovar Typhi a cluster of four genes encoding a deoxyribokinase (DeoK), a putative permease (DeoP), a repressor (DeoQ), and an open reading frame encoding a 337 amino acid residues protein of unknown function. We show that the latter protein, called DeoM, is a hexamer whose synthesis is increased by a factor over 5 after induction with deoxyribose. The CD spectrum of the purified recombinant protein indicated a dominant contribution of {beta}type secondary structure and a small content of {alpha}-helix. Temperature and guanidinium hydrochloride induced denaturation of DeoM indicated that the hexamer dissociation and monomer unfolding are coupled processes. DeoM exhibits 12.5% and 15% sequence identity with galactose mutarotase from Lactococcus lactis and respectively Escherichia coli, which suggested that these three proteins share similar functions. Polarimetric experiments demonstrated that DeoM is a mutarotase with high specificity for deoxyribose. Site-directed mutagenesis of His183 in DeoM, corresponding to a catalytically active residue in GalM, yielded an almost inactive deoxyribose mutarotase. DeoM was crystallized and diffraction data collected for two crystal systems, confirmed its hexameric state. The possible role of the protein and of the entire gene cluster is discussed in connection with the energy metabolism of S. enterica under particular growth conditions.

Keywords: Salmonella enterica; DeoM protein; deoxyribose mutarotase; site-directed mutagenesis; structural characterization

Reprint requests to: Anne-Marie Gilles, Unité de Génétique des Génomes Bactériens, Institut Pasteur, 28, rue du Dr. Roux, 75724 Paris cedex 15, France; e-mail: amgilles{at}pasteur.fr; fax: 33 (1) 45-68-89-48.

7 Present addresses: Unité de Génétique des Génomes Bactériens, Institut Pasteur, 28, rue du Dr. Roux, 75724 Paris cedex 15, France;

8 Centre for Molecular Microbiology and Infection, Imperial College, London, United Kingdom.

Article published ahead of print. Article and publication date are at http://www.proteinscience.org/cgi/doi/10.1110/ps.03566004.


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