HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

J. Biol. Chem., Vol. 282, Issue 5, 3367-3378, February 2, 2007

This Article Full Text Full Text (PDF) All Versions of this Article: 282/5/3367    most recent M605007200v1 Submit a Letter to Editor Alert me when this article is cited Alert me when eLetters are posted Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Request Permissions Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Rouhier, N. Articles by Boschi-Muller, S. Search for Related Content PubMed PubMed Citation Articles by Rouhier, N. Articles by Boschi-Muller, S. Social Bookmarking                      What's this?

Functional and Structural Aspects of Poplar Cytosolic and Plastidial Type A Methionine Sulfoxide Reductases^*

Nicolas Rouhier¹², Brice Kauffmann¹, Frédérique Tete-Favier, Pasquale Palladino, Pierre Gans^¶, Guy Branlant^||, Jean-Pierre Jacquot, and Sandrine Boschi-Muller^||

From the UMR 1136 INRA-UHP, Nancy Universités, Interactions Arbres Microorganismes, IFR 110, Faculté des Sciences et Techniques, BP 239, 54506 Vandoeuvre Cedex, UMR 7036 CNRS-UHP, Nancy Universités, LCM3B, Groupe de Biocristallographie, Faculté des Sciences et Techniques, BP 239, 54506 Vandoeuvre Cedex, ^¶Laboratoire de Résonance Magnétique Nucléaire, Institut de Biologie Structurale, CEA-CNRS-UJF "Jean-Pierre Ebel," 38027 Grenoble Cedex 1, and ^||UMR 7567 CNRS-UHP, Nancy Universités, Laboratoire MAEM, Groupe Enzymologie Moléculaire, Faculté des Sciences et Techniques, BP 239, 54506 Vandoeuvre Cedex, France

The genome of Populus trichocarpa contains five methionine sulfoxide reductase A genes. Here, both cytosolic (cMsrA) and plastidial (pMsrA) poplar MsrAs were analyzed. The two recombinant enzymes are active in the reduction of methionine sulfoxide with either dithiothreitol or poplar thioredoxin as a reductant. In both enzymes, five cysteines, at positions 46, 81, 100, 196, and 202, are conserved. Biochemical and enzymatic analyses of the cysteine-mutated MsrAs support a catalytic mechanism involving three cysteines at positions 46, 196, and 202. Cys⁴⁶ is the catalytic cysteine, and the two C-terminal cysteines, Cys¹⁹⁶ and Cys²⁰², are implicated in the thioredoxin-dependent recycling mechanism. Inspection of the pMsrA x-ray three-dimensional structure, which has been determined in this study, strongly suggests that contrary to bacterial and Bos taurus MsrAs, which also contain three essential Cys, the last C-terminal Cys²⁰², but not Cys¹⁹⁶, is the first recycling cysteine that forms a disulfide bond with the catalytic Cys⁴⁶. Then Cys²⁰² forms a disulfide bond with the second recycling cysteine Cys¹⁹⁶ that is preferentially reduced by thioredoxin. In agreement with this assumption, Cys²⁰² is located closer to Cys⁴⁶ compared with Cys¹⁹⁶ and is included in a ²⁰²CYG²⁰⁴ signature specific for most plant MsrAs. The tyrosine residue corresponds to the one described to be involved in substrate binding in bacterial and B. taurus MsrAs. In these MsrAs, the tyrosine residue belongs to a similar signature as found in plant MsrAs but with the first C-terminal cysteine instead of the last C-terminal cysteine.

Received for publication, May 24, 2006 , and in revised form, November 15, 2006.

The atomic coordinates and structure factors (code 2J89) have been deposited in the Protein Data Bank, Research Collaboratory for Structural Bioinformatics, Rutgers University, New Brunswick, NJ (http://www.rcsb.org/).

The nucleotide sequence(s) reported in this paper has been submitted to the GenBank^TM/EBI Data Bank with accession number(s) AAS46231 [GenBank] and AAS46232 [GenBank] .

^* 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.

¹ Both authors contributed equally to this work.

² To whom correspondence should be addressed. Tel.: 33-3-83684225; E-mail: nrouhier{at}scbiol.uhp-nancy.fr.

CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				L. Tarrago, E. Laugier, M. Zaffagnini, C. Marchand, P. Le Marechal, N. Rouhier, S. D. Lemaire, and P. Rey Regeneration Mechanisms of Arabidopsis thaliana Methionine Sulfoxide Reductases B by Glutaredoxins and Thioredoxins J. Biol. Chem., July 10, 2009; 284(28): 18963 - 18971. [Abstract] [Full Text] [PDF]

				L. Tarrago, E. Laugier, and P. Rey Protein-Repairing Methionine Sulfoxide Reductases in Photosynthetic Organisms: Gene Organization, Reduction Mechanisms, and Physiological Roles Mol Plant, March 1, 2009; 2(2): 202 - 217. [Abstract] [Full Text] [PDF]

				A. Gand, M. Antoine, S. Boschi-Muller, and G. Branlant Characterization of the Amino Acids Involved in Substrate Specificity of Methionine Sulfoxide Reductase A J. Biol. Chem., July 13, 2007; 282(28): 20484 - 20491. [Abstract] [Full Text] [PDF]