We describe a novel protein Ser/Thr phosphatase from Arabidopsis thaliana, PP7, which is only 27-32% identical in amino acid sequence to the known phosphatases and is the most divergent member of the PPP (PP1/2A/2B) family for today. Some structural features suggest more close relationship of PP7 to the PP5/rdgC subfamily. PP7 contains all of the residues essential for the phosphatase activity and possesses three major insertions in its presumable C-terminal subdomain, which suggest its unique regulation and/or optimisation of its structure for interaction with specific substrates or regulators. A phosphatase structurally related to PP7 is expressed in rice. PP7 conservation between mono- and dicotyledonous plants may point to its essential role in the plant cell.
CITATION STYLE
Andreeva, A. V., Evans, D. E., Hawes, C. R., Bennett, N., & Kutuzov, M. A. (1998). PP7, a plant phosphatase representing a novel evolutionary branch of eukaryotic protein Ser/Thr phosphatases. Biochemistry and Molecular Biology International, 44(4), 703–715. https://doi.org/10.1080/15216549800201752
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