TAILIEUCHUNG - Báo cáo Y học: The Saccharomyces cerevisiae type 2A protein phosphatase Pph22p is biochemically different from mammalian PP2A

The Saccharomyces cerevisiae type 2A protein phosphatase (PP2A) Pph22p differs from the catalytic subunits of PP2A (PP2Ac) present in mammals, plants and Schizosaccharomyces pombe by a unique N-terminal extension of approximately 70 amino acids. We have overexpressed S. cerevisiae Pph22p and its N-terminal deletion mutant DN-Pph22p in the GS115 strain of Pichia pastoris and purified these enzymes to apparent homogeneity. | Eur. J. Biochem. 269 3372-3382 2002 FEBS 2002 doi The Saccharomyces cerevisiae type 2A protein phosphatase Pph22p is biochemically different from mammalian PP2A Piotr Zabrocki1 Wojciech Swiatek1 Ewa Sugajska1 Johan M. Thevelein2 Stefaan Wera2 and Stanislaw Zolnierowicz1 1Cell and Molecular Signaling Laboratory Intercollegiate Faculty of Biotechnology UG-MUG Gdansk Poland 2Laboratorium voor Moleculaire Celbiologie . Leuven Leuven-Heverlee Flanders Belgium The Saccharomyces cerevisiae type 2A protein phosphatase PP2A Pph22p differs from the catalytic subunits of PP2A PP2Ac present in mammals plants and Schizosaccharom-yces pombe by a unique N-terminal extension of approximately 70 amino acids. We have overexpressed S. cerevisiae Pph22p and its N-terminal deletion mutant DN-Pph22p in the GS115 strain of Pichia pastoris and purified these enzymes to apparent homogeneity. Similar to other heterologous systems used to overexpress PP2Ac a low yield of an active enzyme was obtained. The recombinant enzymes designed with an 8 X His-tag at their N-terminus were purified by ion-exchange chromatography on DEAE-Sephacel and affinity chromatography on Ni2 -nitrilotri-acetic acid agarose. Comparison of biochemical properties of purified Pph22p and DN-Pph22p with purified human 8 X His PP2Ac identified similarities and differences between these two enzymes. Both enzymes displayed similar specific activities with 32P-labelled phosphorylase a as substrate. Furthermore selected inhibitors and metal ions affected their activities to the same extend. In contrast to the mammalian catalytic subunit PP2Ac but similar to the dimeric form of mammalian PP2A Pph22p but not DN-Pph22p interacted strongly with protamine. Also with regard to the effects of protamine and polylysine on phosphatase activity Pph22p but not DN-Pph22p behaved similarly to the PP2Ac-PR65 dimer indicating a regulatory role for the N-terminal extension of Pph22p. The N-terminal .

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