Please use this identifier to cite or link to this item: http://hdl.handle.net/10174/5780

Title: CGDEase, a Pseudomonas fluorescens protein of the PLC/APase superfamily with CDP-ethanolamine and (dihexanoyl) glycerophosphoethanolamine hydrolase activity induced by osmoprotectants under phosphate-deficient conditions
Authors: Costas, MJ
Cordero, PM
Cabezas, A
Alves-Pereira, I
Cameselle, C
Ribeiro, JM
Keywords: Pseudomonas fluorescens
CDP-ethanolamine pyrophosphatase/ (dihexanoyl)glycerophosphoethanolamine phosphodiesterase
PLC/APase
Issue Date: Oct-2010
Citation: Costas MJ, Pinto RM, Cordero PM, Cabezas A, Alves-Pereira I, Cameselle C, Ribeiro JM (2010) CGDEase, a Pseudomonas fluorescens protein of the PLC/APase superfamily with CDP-ethanolamine and (dihexanoyl) glycerophosphoethanolamine hydrolase activity induced by osmoprotectants under phosphate-deficient conditions. Molecular microbiology, 78:1556-1576. doi: 10.1111/j.1365-2958.2010.07425.x
Abstract: A novel enzyme, induced by choline, ethanolamine, glycine betaine or dimethylglycine, was released at low temperature and phosphate from Pseudomonas fluorescens (CECT 7229) suspensions at low cell densities. It is a CDP-ethanolamine pyrophosphatase/(dihexanoyl)glycerophosphoethanolamine phosphodiesterase (CGDEase) less active on choline derivatives, and inactive on long-chain phospholipids, CDP-glycerol and other NDP-X compounds. The reaction pattern was typical of phospholipase C (PLC), as either phosphoethanolamine or phosphocholine was produced. Peptide-mass analyses, gene cloning and expression provided a molecular identity for CGDEase. Bioinformatic studies assigned it to the PLC branch of the phospholipase C/acid phosphatase (PLC/APase) superfamily, revealed an irregular phylogenetic distribution of close CGDEase relatives, and suggested their genes are not in operons or conserved contexts. A theoretical CGDEase structure was supported by mutagenesis of two predicted active-site residues, which yielded essentially inactive mutants. Biological relevance is supported by comparisons with CGDEase relatives, induction by osmoprotectants (not by osmotic stress itself) and repression by micromolar phosphate. The low bacterial density requirement was related to phosphate liberation from lysed bacteria in denser populations, rather than to a classical quorum-sensing effect. The results fit better a CGDEase role in phosphate scavenging than in osmoprotection.
URI: http://onlinelibrary.wiley.com/doi/10.1111/j.1365-2958.2010.07425.x/abstract
http://hdl.handle.net/10174/5780
Type: article
Appears in Collections:QUI - Publicações - Artigos em Revistas Internacionais Com Arbitragem Científica
ICAAM - Publicações - Artigos em Revistas Internacionais Com Arbitragem Científica

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