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Updated: Aug 15, 2026

Recombinant α- β- and γ-Synucleins Stimulate Protein Phosphatase 2A Catalytic Subunit Activity in Cell Free Assays
Published on: August 13, 2017
[Serine-threonine protein phosphatases from Bacillus subtilis]
1Medical University of Gdansk, Intercollegiate Faculty of Biotechnology UG-AMG, Department of Cell Biology, 1 Debinki St., 80-811 Gdansk, Poland. obuchowk@biotech.univ.gda.pl
Abstract:
Gram-positive soil bacterium Bacillus subtilis possesses six eukaryotic-like serine-threonine protein phosphatases. These enzymes play an important role in the cell. The response to environmental or nutrional stress conditions are controlled by three Rsb phosphatases: RsbX, RsbU and RsbP. Phosphatases are also involved in endospore formation process (SpoIIE) and sugar transport (kinase/phosphatase Hpr). Moreover in the cell there are phosphatases with still unknown function (PrpC and PrpE). Cellular processes, presented here are regulated by serine/threonine protein phosphatases and very important for bacterial survival in natural environment. Protein phosphatases must act in cooperation with protein kinases and deserve the same attention as kinases.
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