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

FEBS Letters

Meek, Sarah¹  Morrice, Nick¹  MacKintosh, Carol¹ 

[1] Medical Research Council Protein Phosphorylation Unit, Department of Biochemistry, University of Dundee, MSI/WTB Complex, Dundee DD1 5EH, UK

关键词: Arachidonic acid;    Protein phosphatase 5;    Tetratricopeptide repeat;    Plant;   

DOI  :  10.1016/S0014-5793(99)01093-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown