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

J. Biol. Chem., Vol. 282, Issue 30, 21738-21745, July 27, 2007

This Article Full Text Full Text (PDF) All Versions of this Article: 282/30/21738    most recent M703536200v1 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 Jerga, A. Articles by Rock, C. O. Search for Related Content PubMed PubMed Citation Articles by Jerga, A. Articles by Rock, C. O. Social Bookmarking                      What's this?

Identification of a Soluble Diacylglycerol Kinase Required for Lipoteichoic Acid Production in Bacillus subtilis^*

Agoston Jerga, Ying-Jie Lu¹, Gustavo E. Schujman², Diego de Mendoza²³, and Charles O. Rock⁴

From the Department of Infectious Diseases, St. Jude Children's Research Hospital, Memphis, Tennessee 38105-2794 and Instituto de Biología Molecular y Celular de Rosario and Departamento de Microbiología, Facultad de Ciencias Bioquímicas y Farmacéuticas, Universidad Nacional de Rosario, Rosario, Argentina

Diacylglycerol kinases (DagKs) are key enzymes in lipid metabolism that function to reintroduce diacylglycerol formed from the hydrolysis of phospholipids into the biosynthetic pathway. Bacillus subtilis is a prototypical Gram-positive bacterium with a lipoteichoic acid structure containing repeating units of sn-glycerol-1-P groups derived from phosphatidylglycerol head groups. The B. subtilis homolog of the prokaryotic DagK gene family (dgkA; Pfam01219) was not a DagK but rather was an undecaprenol kinase. The three members of the soluble DagK protein family (Pfam00781) in B. subtilis were tested by complementation of an E. coli dgkA mutant, and only the essential yerQ gene possessed DagK activity. This gene was dubbed dgkB, and the soluble protein product was purified, and its DagK activity was verified in vitro. Conditional inactivation of dgkB led to the accumulation of diacylglycerol and the cessation of lipoteichoic acid formation in B. subtilis. This study identifies a soluble protein encoded by the dgkB (yerQ) gene as an essential kinase in the diacylglycerol cycle that drives lipoteichoic acid production.

Received for publication, April 27, 2007 , and in revised form, May 24, 2007.

Note Added in Proof—After submission of our paper, we became aware of a much more relevant and recent study (29).

^* This work was supported by National Institutes of Health Grant GM34496 (to C. O. R.), Cancer Center Support Grant CA 21765, Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET, Argentina), Agencia de Promoción Científica y Tecnológica (FONCYT, Argentina), and the American Lebanese Syrian Associated Charities. 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 Present address: Division of Infectious Diseases, Children's Hospital, Boston, MA 02115.

² Career Investigator at CONICET.

³ An International Research Scholar of the Howard Hughes Medical Institute.

⁴ To whom correspondence should be addressed: Dept. of Infectious Diseases, St. Jude Children's Research Hospital, 332 N. Lauderdale, Memphis, TN 38105-2794. Tel.: 901-495-3491; Fax: 901-495-0399; E-mail: charles.rock{at}stjude.org.

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

This article has been cited by other articles:

				A. Jerga, D. J. Miller, S. W. White, and C. O. Rock Molecular Determinants for Interfacial Binding and Conformational Change in a Soluble Diacylglycerol Kinase J. Biol. Chem., March 13, 2009; 284(11): 7246 - 7254. [Abstract] [Full Text] [PDF]

				L. I. Salzberg and J. D. Helmann Phenotypic and Transcriptomic Characterization of Bacillus subtilis Mutants with Grossly Altered Membrane Composition J. Bacteriol., December 1, 2008; 190(23): 7797 - 7807. [Abstract] [Full Text] [PDF]

				V. R. F. Matias and T. J. Beveridge Lipoteichoic Acid Is a Major Component of the Bacillus subtilis Periplasm J. Bacteriol., November 15, 2008; 190(22): 7414 - 7418. [Abstract] [Full Text] [PDF]