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Dephosphorylation of the phosphoprotein P(II) in Synechococcus PCC 7942: identification of an ATP and 2-oxoglutarate-regulated phosphatase activity.
Irmler, A; Sanner, S; Dierks, H; Forchhammer, K.
Afiliación
  • Irmler A; Lehrstuhl für Mikrobiologie der Universität München, Munich, Germany.
Mol Microbiol ; 26(1): 81-90, 1997 Oct.
Article en En | MEDLINE | ID: mdl-9383191
The phosphorylation state of the putative signal transduction protein P(II) from the cyanobacterium Synechococcus sp. strain PCC 7942 depends on the cellular state of nitrogen and carbon assimilation. In this study, dephosphorylation of phosphorylated P(II) protein (P[II]-P) was investigated both in vivo and in vitro. The in vivo studies implied that P(II)-P dephosphorylation is regulated by inhibitory metabolites involved in the glutamine synthetase-glutamate synthase pathway of ammonium assimilation. An in vitro assay for P(II)-P dephosphorylation was established that revealed a Mg2+-dependent P(II)-P phosphatase activity. P(II)-P phosphatase and P(II) kinase activities could be separated biochemically. A partially purified P(II)-P phosphatase preparation also catalysed the dephosphorylation of phosphoserine/phosphothreonine residues on other proteins in a Mg2+-dependent manner. However, only dephosphorylation of P(II)-P was regulated by synergistic inhibition by ATP and 2-oxoglutarate. As the same metabolites stimulate the P(II) kinase activity, it appears that the phosphorylation state of P(II) is determined by ATP and 2-oxoglutarate-dependent reciprocal reactivity of P(II) towards its phosphatase and kinase.
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Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Proteínas Bacterianas / Adenosina Trifosfato / Cianobacterias / Fosfoproteínas Fosfatasas / Ácidos Cetoglutáricos Tipo de estudio: Diagnostic_studies Idioma: En Revista: Mol Microbiol Asunto de la revista: BIOLOGIA MOLECULAR / MICROBIOLOGIA Año: 1997 Tipo del documento: Article País de afiliación: Alemania Pais de publicación: Reino Unido
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Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Proteínas Bacterianas / Adenosina Trifosfato / Cianobacterias / Fosfoproteínas Fosfatasas / Ácidos Cetoglutáricos Tipo de estudio: Diagnostic_studies Idioma: En Revista: Mol Microbiol Asunto de la revista: BIOLOGIA MOLECULAR / MICROBIOLOGIA Año: 1997 Tipo del documento: Article País de afiliación: Alemania Pais de publicación: Reino Unido