Microbiology
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


Microbiology 151 (2005), 3071-3080; DOI  10.1099/mic.0.27958-0
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via CrossRef
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Cullinane, M.
Right arrow Articles by O'Gara, F.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Cullinane, M.
Right arrow Articles by O'Gara, F.
Agricola
Right arrow Articles by Cullinane, M.
Right arrow Articles by O'Gara, F.
Microbiology 151 (2005), 3071-3080; DOI  10.1099/mic.0.27958-0
© 2005 Society for General Microbiology

Identification of two lysophosphatidic acid acyltransferase genes with overlapping function in Pseudomonas fluorescens

Méabh Cullinane, Christine Baysse, John P. Morrissey and Fergal O'Gara

BIOMERIT Research Centre, Microbiology Department and Biosciences Institute, National University of Ireland, Cork, Ireland

Correspondence
Fergal O'Gara
f.ogara{at}ucc.ie

Phosphatidic acid (PA) is known to be a crucial phospholipid intermediate in cell membrane biosynthesis. In Escherichia coli, this molecule is produced from lysophosphatidic acid (LPA) by LPA acyltransferase (EC 2.3.1.51), encoded by plsC. E. coli possesses only one such LPA acyltransferase and a plsC mutant is non-permissive for growth at elevated temperatures. This study describes the identification and characterization of two genes from Pseudomonas fluorescens F113 that encode enzymes with LPA acyltransferase activity. One of the genes, hdtS, was previously described, whereas patB is a novel gene. In addition, a putative lyso-ornithine lipid acyltransferase was also identified. All three proteins possess conserved acyltransferase domains and are homologous to PlsC and to LPA acyltransferases identified in Neisseria meningitidis. Functional analysis determined that both HdtS and PatB are functional LPA acyltransferases, as both complemented an E. coli plsC mutant. Mutants lacking each of the putative acyltransferases were constructed and analysed. Growth defects were observed for hdtS and patB single mutants, and a double hdtSpatB mutant could not be constructed. To determine precise roles in phospholipid synthesis, fatty acid methyl ester analysis was carried out. The hdtS mutant displayed a profile consistent with a defect in LPA acyltransferase activity, whereas no such phenotype was observed in the patB mutant, indicating that hdtS encodes the primary LPA acyltransferase in the cell. The presence of at least two genes specifying LPA acyltransferase activity may have implications for the function and survival of P. fluorescens in diverse environments.


Abbreviations: acyl-ACP, acyl-acyl carrier protein; acyl-CoA, acyl-coenzyme A; FAME, fatty acid methyl ester; LPA, lysophosphatidic acid

The GenBank/EMBL/DDBJ accession numbers for the genes reported in this paper are: pasA, DQ088968; olsA, AY876048; patB, AY876049; hdtS, AF286536.




This article has been cited by other articles:


Home page
J. Lipid Res.Home page
Y.-M. Zhang and C. O. Rock
Thematic Review Series: Glycerolipids. Acyltransferases in bacterial glycerophospholipid synthesis
J. Lipid Res., September 1, 2008; 49(9): 1867 - 1874.
[Abstract] [Full Text] [PDF]


Home page
MicrobiologyHome page
P. Williams
Quorum sensing, communication and cross-kingdom signalling in the bacterial world
Microbiology, December 1, 2007; 153(12): 3923 - 3938.
[Abstract] [Full Text] [PDF]


Home page
J. Bacteriol.Home page
S. Aygun-Sunar, R. Bilaloglu, H. Goldfine, and F. Daldal
Rhodobacter capsulatus OlsA Is a Bifunctional Enyzme Active in both Ornithine Lipid and Phosphatidic Acid Biosynthesis
J. Bacteriol., December 1, 2007; 189(23): 8564 - 8574.
[Abstract] [Full Text] [PDF]


Home page
Appl. Environ. Microbiol.Home page
M. Rivas, M. Seeger, E. Jedlicki, and D. S. Holmes
Second Acyl Homoserine Lactone Production System in the Extreme Acidophile Acidithiobacillus ferrooxidans
Appl. Envir. Microbiol., May 15, 2007; 73(10): 3225 - 3231.
[Abstract] [Full Text] [PDF]


Home page
Microbiol. Mol. Biol. Rev.Home page
Y. Xu, B. Labedan, and N. Glansdorff
Surprising Arginine Biosynthesis: a Reappraisal of the Enzymology and Evolution of the Pathway in Microorganisms
Microbiol. Mol. Biol. Rev., March 1, 2007; 71(1): 36 - 47.
[Abstract] [Full Text] [PDF]


Home page
J. Virol.Home page
D. K. Bideshi, M.-V. Demattei, F. Rouleux-Bonnin, K. Stasiak, Y. Tan, S. Bigot, Y. Bigot, and B. A. Federici
Genomic Sequence of Spodoptera frugiperda Ascovirus 1a, an Enveloped, Double-Stranded DNA Insect Virus That Manipulates Apoptosis for Viral Reproduction
J. Virol., December 1, 2006; 80(23): 11791 - 11805.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
INT J SYST EVOL MICROBIOL MICROBIOLOGY J GEN VIROL
J MED MICROBIOL ALL SGM JOURNALS
Copyright © 2005 Society for General Microbiology.