Microcystin affinity purification of plant protein phosphatases: PP1C, PP5 and a regulatory A-subunit of PP2A

Meek, S., Morrice, N. and MacKintosh, C. (1999) Microcystin affinity purification of plant protein phosphatases: PP1C, PP5 and a regulatory A-subunit of PP2A. FEBS Letters, 457(3), pp. 494-498. (doi:10.1016/S0014-5793(99)01093-5)

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Publisher's URL: http://dx.doi.org/10.1016/S0014-5793(99)01093-5

Abstract

Proteins of ∼35, 55 and 65 kDa were purified from cauliflower extracts by microcystin-Sepharose chromatography and identified by amino acid sequencing as plant forms of protein (serine/threonine) phosphatase 1 (PP1) catalytic subunit, PP5 and a regulatory A-subunit of PP2A, respectively. Peptides that corresponded both to the tetratricopeptide (TPR) repeat and catalytic domains of PP5 were identified. Similar to mammalian PP5, the casein phosphatase activity of plant PP5 was activated >10-fold by arachidonic acid, with half-maximal stimulation occurring at ∼100 μM lipid.

Item Type:Articles
Status:Published
Refereed:Yes
Glasgow Author(s) Enlighten ID:Meek, Dr Sarah
Authors: Meek, S., Morrice, N., and MacKintosh, C.
College/School:College of Medical Veterinary and Life Sciences > School of Medicine, Dentistry & Nursing
Journal Name:FEBS Letters
Publisher:Federation of European Biochemical Societies
ISSN:0014-5793
ISSN (Online):1873-3468

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