Multiple protein-aspartate phosphatases provide a mechanism for the integration of diverse signals in the control of development in B. subtilis
Identifieur interne : 001327 ( Istex/Curation ); précédent : 001326; suivant : 001328Multiple protein-aspartate phosphatases provide a mechanism for the integration of diverse signals in the control of development in B. subtilis
Auteurs : Marta Perego ; Conrad Hanstein ; Katherine M. Welsh [États-Unis] ; Tsotne Djavakhishvili [États-Unis] ; Philippe Glaser [France] ; James A. Hoch [États-Unis]Source :
- Cell [ 0092-8674 ] ; 1994.
Abstract
Abstract: The initiation of sporulation in B. subtilis is regulated by the Spo0A transcription factor, which is activated by phosphorylation to control developmental switching from the vegetative to the sporulation state. The level of phosphorylation of Spo0A is regulated by the phosphorelay, a signal transduction system based on the protein-histidine kinase-response regulator two-component paradigm. To initiate sporulation, the cell must recognize and interpret a large variety of environmental, metabolic, and cell cycle signals that influence the phosphorylation level of Spo0A. We describe here a family of protein-aspartate phosphatases with activity of Spo0F∼P, a response regulator component of the phosphorelay, that provide a mechanism for signal recognition and interpretation. These phosphatases function to drain the phosphorelay, lower Spo0A∼P levels, and prevent sporulation. The integration of diverse environmental signals that affect the initiation of sporulation likely occurs through the competition between opposing activities of protein kinases and protein phosphatases.
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DOI: 10.1016/0092-8674(94)90035-3
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Marta Perego<affiliation><mods:affiliation>Dipartimento Farmaceutico Universita′ degli Studi diP´arma Via delle Scienze 43100 Parma Italy</mods:affiliation><wicri:noCountry code="no comma">Dipartimento Farmaceutico Universita′ degli Studi diP´arma Via delle Scienze 43100 Parma Italy</wicri:noCountry></affiliation><affiliation><mods:affiliation>Dipartimento di Genetica e Microbiologia “A. Buzzati Traverso” Universita′ degli Studi di Pavia 27100 Pavia Italy</mods:affiliation><wicri:noCountry code="no comma">Dipartimento di Genetica e Microbiologia “A. Buzzati Traverso” Universita′ degli Studi di Pavia 27100 Pavia Italy</wicri:noCountry></affiliation>Le document en format XML
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Buzzati Traverso” Universita′ degli Studi di Pavia 27100 Pavia Italy</mods:affiliation><wicri:noCountry code="no comma">Dipartimento di Genetica e Microbiologia “A. Buzzati Traverso” Universita′ degli Studi di Pavia 27100 Pavia Italy</wicri:noCountry></affiliation></author><author><name sortKey="Welsh, Katherine M" sort="Welsh, Katherine M" uniqKey="Welsh K" first="Katherine M." last="Welsh">Katherine M. 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The level of phosphorylation of Spo0A is regulated by the phosphorelay, a signal transduction system based on the protein-histidine kinase-response regulator two-component paradigm. To initiate sporulation, the cell must recognize and interpret a large variety of environmental, metabolic, and cell cycle signals that influence the phosphorylation level of Spo0A. We describe here a family of protein-aspartate phosphatases with activity of Spo0F∼P, a response regulator component of the phosphorelay, that provide a mechanism for signal recognition and interpretation. These phosphatases function to drain the phosphorelay, lower Spo0A∼P levels, and prevent sporulation. The integration of diverse environmental signals that affect the initiation of sporulation likely occurs through the competition between opposing activities of protein kinases and protein phosphatases.</div></front></TEI></record>Pour manipuler ce document sous Unix (Dilib)
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