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J. Biol. Chem., Vol. 281, Issue 34, 24462-24471, August 25, 2006

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A New Rubisco-like Protein Coexists with a Photosynthetic Rubisco in the Planktonic Cyanobacteria Microcystis^*

Alyssa Carré-Mlouka¹, Annick Méjean, Philippe Quillardet, Hiroki Ashida, Yohtaro Saito, Akiho Yokota, Isabelle Callebaut^¶, Agnieszka Sekowska^||2, Elke Dittmann^**, Christiane Bouchier, and Nicole Tandeau de Marsac³

From the Département de Microbiologie, Unité des Cyanobactéries (CNRS-URA 2172) and Plate-forme Génomique-Pasteur Génopole Ile de France, Institut Pasteur, 28 rue du Docteur Roux, 75724 Paris Cedex 15, France, the Nara Institute of Science and Technology (NAIST), Graduate School of Biological Sciences, 8916-5 Takayama, Ikoma, Nara 630-0101, Japan, the ^¶Département de Biologie Structurale, Institut de Minéralogie et Physique des Milieux Condensés, CNRS UMR7590, Universités Paris 6 et 7, case 115, 4 place Jussieu, 75252 Paris Cedex 05, France, the ^||HKU-Pasteur Research Centre, Dexter HC Man Building, 8 Sassoon Road, Pokfulam, Hong Kong, China, and the ^**Institute of Biology, Humboldt University, Chausseestrasse 117, 10115 Berlin, Germany

Two genes encoding proteins related to large subunits of Rubisco were identified in the genome of the planktonic cyanobacterium Microcystis aeruginosa PCC 7806 that forms water blooms worldwide. The rbcL_I gene belongs to the form I subfamily typically encountered in cyanobacteria, green algae, and land plants. The second and newly discovered gene is of the form IV subfamily and widespread in the Microcystis genus. In M. aeruginosa PCC 7806 cells, the expression of both rbcL_I and rbcL_IV is sulfur-dependent. The purified recombinant RbcL_IV overexpressed in Escherichia coli cells did not display CO₂ fixation activity but catalyzed enolization of 2,3-diketo-5-methylthiopentyl-1-phosphate, and the rbcL_IV gene rescued a Bacillus subtilis MtnW-deficient mutant. Therefore, the Microcystis RbcL_IV protein functions both in vitro and in vivo and might be involved in a methionine salvage pathway. Despite variations in the amino acid sequences, RbcL_IV shares structural similarities with all members of the Rubisco superfamily. Invariant amino acids within the catalytic site may thus represent the minimal set for enolization, whereas variations, especially located in loop 6, may account for the limitation of the catalytic reaction to enolization. Even at low protein concentrations in vitro, the recombinant RbcL_IV assembles spontaneously into dimers, the minimal unit required for Rubisco forms I–III activity. The discovery of the coexistence of RbcL_I and RbcL_IV in cyanobacteria, the ancestors of chloroplasts, enlightens episodes of the chaotic evolutionary history of the Rubiscos, a protein family of major importance for life on Earth.

Received for publication, March 29, 2006 , and in revised form, May 24, 2006.

^* This work was supported by the Institut Pasteur, the CNRS (URA 2172), the Ministère de l'Education Nationale, de la Recherche et de la Technologie (MENRT), and the University Paris 7-Denis Diderot. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The on-line version of this article (available at http://www.jbc.org) contains supplemental figures and tables.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBank^TM/EBI Data Bank with accession number(s) AM157793 [GenBank] for rbcL_I and AM157794 [GenBank] for rbcL_IV.

¹ Recipient of a Ph.D. fellowship from the MENRT. Present address: Laboratoire de Génétique et Biologie Cellulaire, Université Versailles-Saint Quentin en Yvelines, 45 avenue des Etats-Unis, 78035 Versailles Cedex, France.

² Present address: Laboratoire de Signalisation, Phosphoprotéome et Communautés Bactériennes, Institut de Génétique et Microbiologie, CNRS UMR8621, Bât. 409, Université Paris-Sud, 91405 Orsay Cedex, France.

³ To whom correspondence should be addressed. Tel.: 33-1-45-68-84-15; Fax: 33-1-40-61-30-42; E-mail: ntmarsac{at}pasteur.fr.

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