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

J. Biol. Chem., Vol. 283, Issue 26, 18099-18112, June 27, 2008

This Article Full Text Full Text (PDF) An addition or correction has been published All Versions of this Article: 283/26/18099    most recent M802615200v1 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 Fiuza, M. Articles by Molle, V. Search for Related Content PubMed PubMed Citation Articles by Fiuza, M. Articles by Molle, V. Social Bookmarking                      What's this?

From the Characterization of the Four Serine/Threonine Protein Kinases (PknA/B/G/L) of Corynebacterium glutamicum toward the Role of PknA and PknB in Cell Division^*

Maria Fiuza¹, Marc J. Canova, Isabelle Zanella-Cléon, Michel Becchi, Alain J. Cozzone, Luís M. Mateos, Laurent Kremer^¶||, José A. Gil, and Virginie Molle²

From the Departamento de Biología Molecular, Á_rea de Microbiología, Facultad de Biología, Universidad de León, León 24071, Spain, the Institut de Biologie et Chimie des Protéines, UMR 5086, CNRS, Université Lyon 1, IFR128 BioSciences, Lyon-Gerland, 7 Passage du Vercors, 69367 Lyon Cedex 07, France, the ^¶Laboratoire de Dynamique des Interactions Membranaires Normales et Pathologiques, Université de Montpellier II et I, CNRS, UMR 5235, Case 107, Place Eugène Bataillon, 34095 Montpellier Cedex 05, France, and ^||INSERM, DIMNP, Place Eugène Bataillon, 34095 Montpellier Cedex 05, France

Corynebacterium glutamicum contains four serine/threonine protein kinases (STPKs) named PknA, PknB, PknG, and PknL. Here we present the first biochemical and comparative analysis of all four C. glutamicum STPKs and investigate their potential role in cell shape control and peptidoglycan synthesis during cell division. In vitro assays demonstrated that, except for PknG, all STPKs exhibited autokinase activity. We provide evidence that activation of PknG is part of a phosphorylation cascade mechanism that relies on PknA activity. Following phosphorylation by PknA, PknG could transphosphorylate its specific substrate OdhI in vitro. A mass spectrometry profiling approach was also used to identify the phosphoresidues in all four STPKs. The results indicate that the nature, number, and localization of the phosphoacceptors varies from one kinase to the other. Disruption of either pknL or pknG in C. glutamicum resulted in viable mutants presenting a typical cell morphology and growth rate. In contrast, we failed to obtain null mutants of pknA or pknB, supporting the notion that these genes are essential. Conditional mutants of pknA or pknB were therefore created, leading to partial depletion of PknA or PknB. This resulted in elongated cells, indicative of a cell division defect. Moreover, overexpression of PknA or PknB in C. glutamicum resulted in a lack of apical growth and therefore a coccoid-like morphology. These findings indicate that pknA and pknB are key players in signal transduction pathways for the regulation of the cell shape and both are essential for sustaining corynebacterial growth.

Received for publication, April 3, 2008 , and in revised form, April 24, 2008.

^* This work was supported in part by grants from the Region Rhone-Alpes (to M. C.), the CNRS, the University of Lyon (France), National Research Agency Grant ANR-06-MIME-027-01 (to V. M. and L. K.), Junta de Castilla y León Grant LE040A07 (to J. A. G.), and Ministerio de Ciencia y Tecnología (Spain) Grants BIO2008-03234 and BIO2005-02723 (to J. A. G. and L. M. M.). 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 Recipient of a fellowship from the Ministerio de Educación y Ciencia.

² To whom correspondence should be addressed. Tel.: 33-4-72-72-26-79; Fax: 33-4-72-72-26-41; E-mail: vmolle{at}ibcp.fr.

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

This article has been cited by other articles:

				M. Debarbouille, S. Dramsi, O. Dussurget, M.-A. Nahori, E. Vaganay, G. Jouvion, A. Cozzone, T. Msadek, and B. Duclos Characterization of a Serine/Threonine Kinase Involved in Virulence of Staphylococcus aureus J. Bacteriol., July 1, 2009; 191(13): 4070 - 4081. [Abstract] [Full Text] [PDF]

				R. Veyron-Churlet, V. Molle, R. C. Taylor, A. K. Brown, G. S. Besra, I. Zanella-Cleon, K. Futterer, and L. Kremer The Mycobacterium tuberculosis {beta}-Ketoacyl-Acyl Carrier Protein Synthase III Activity Is Inhibited by Phosphorylation on a Single Threonine Residue J. Biol. Chem., March 6, 2009; 284(10): 6414 - 6424. [Abstract] [Full Text] [PDF]

				M. Fiuza, M. J. Canova, D. Patin, M. Letek, I. Zanella-Cleon, M. Becchi, L. M. Mateos, D. Mengin-Lecreulx, V. Molle, and J. A. Gil The MurC Ligase Essential for Peptidoglycan Biosynthesis Is Regulated by the Serine/Threonine Protein Kinase PknA in Corynebacterium glutamicum J. Biol. Chem., December 26, 2008; 283(52): 36553 - 36563. [Abstract] [Full Text] [PDF]