Reference : High inorganic triphosphatase activities in bacteria and mammalian cells: Identification...
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
http://hdl.handle.net/2268/132193
High inorganic triphosphatase activities in bacteria and mammalian cells: Identification of the enzymes involved.
English
Kohn, Grégory [Université de Liège - ULg > > GIGA - Neurosciences >]
Delvaux, David mailto [Université de Liège - ULg > Département des sciences biomédicales et précliniques > GIGA-R : Labo de recherche sur les métastases >]
Lakaye, Bernard mailto [Université de Liège - ULg > Département des sciences biomédicales et précliniques > Biochimie et physiologie humaine et pathologique >]
Servais, Anne-Catherine mailto [Université de Liège - ULg > Département de pharmacie > Analyse des médicaments >]
Scholer, Georges []
Fillet, Marianne mailto [Université de Liège - ULg > Département de pharmacie > Analyse des médicaments >]
Elias, Benjamin []
Derochette, Jean-Michel [Université de Liège - ULg > Département de chimie (sciences) > Chimie analytique et électrochimie >]
Crommen, Jacques mailto [Université de Liège - ULg > Département de pharmacie > Département de pharmacie >]
Wins, Pierre []
Bettendorff, Lucien mailto [Université de Liège - ULg > Département des sciences biomédicales et précliniques > Biochimie et physiologie humaine et pathologique >]
12-Sep-2012
PLoS ONE
Public Library of Science
7
9
e43879
Yes (verified by ORBi)
International
1932-6203
San Franscisco
CA
[en] tripolyphosphate ; Inorganic triphosphatase ; CYTH ; Prune ; CyaB ; Escherichia coli ; thiamine ; exopolyphosphatase ; metastasis
[en] Background: We recently characterized a specific inorganic triphosphatase (PPPase) from Nitrosomonas europaea. This enzyme belongs to the CYTH superfamily of proteins. Many bacterial members of this family are annotated as predicted adenylate cyclases, because one of the founding members is CyaB adenylate cyclase from A. hydrophila. The aim of the present study is to determine whether other members of the CYTH protein family also have a PPPase activity, if there are PPPase activities in animal tissues and what enzymes are responsible for these activities.
Methodology/Principal Findings: Recombinant enzymes were expressed and purified as GST- or His-tagged fusion proteins and the enzyme activities were determined by measuring the release of inorganic phosphate. We show that the hitherto uncharacterized E. coli CYTH protein ygiF is a specific PPPase, but it contributes only marginally to the total PPPase activity in this organism, where the main enzyme responsible for hydrolysis of inorganic triphosphate (PPPi) is inorganic pyrophosphatase. We further show that CyaB hydrolyzes PPPi but this activity is low compared to its adenylate cyclase activity. Finally we demonstrate a high PPPase activity in mammalian and quail tissue, particularly in the brain. We show that this activity is mainly due to Prune, an exopolyphosphatase overexpressed in metastatic tumors where it promotes cell motility.
Conclusions and General Significance: We show for the first time that PPPase activities are widespread in bacteria and animals. We identified the enzymes responsible for these activities but we were unable to detect significant amounts of PPPi in E. coli or brain extracts using ion chromatography and capillary electrophoresis. The role of these enzymes may be to hydrolyze PPPi, which could be cytotoxic because of its high affinity for Ca2+, thereby interfering with Ca2+ signaling.
Giga-Neurosciences
Fonds de la Recherche Scientifique (Communauté française de Belgique) - F.R.S.-FNRS ; Fonds pour la formation à la Recherche dans l'Industrie et dans l'Agriculture (Communauté française de Belgique) - FRIA ; Fonds de la Recherche Fondamentale Collective - FRFC
Researchers ; Professionals ; Students ; General public
http://hdl.handle.net/2268/132193
10.1371/journal.pone.0043879
http://www.plosone.org/article/info%3Adoi%2F10.1371%2Fjournal.pone.0043879

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