QUARTERLY Interaction of maize (Zea mays) protein phosphatase 2A with tubulin

Abstract

maize Immunological and biochemical evidence has been obtained for an interaction of maize protein phosphatase 2A (PP2A) holoenzyme with tubulin. Tubulin co-purifies with maize seedling PP2A. Affinity chromatography of the maize PP2A preparation on immobilized tubulin revealed two peaks of phosphorylase a phosphatase activity. In one of the peaks, the catalytic (C) and constant regulatory (A) subunits of PP2A were identified by Western blotting. The subunits (C and A) of PP2A were co-immunoprecipitated from maize seedlings homogenate by an anti-�-tubulin antibody. The interaction of plant PP2A with tubulin indicates a possible role of reversible protein phosphorylation in the dynamic structure of plant cytoskeleton. Tubulin polymerizes into long chains or filaments that form microtubules, hollow fibers which serve as a skeletal system for living cells. Microtubules (MT) have the ability to shift through various conformations, which enables a cell to undergo mitosis. Mitotic movements of chromosomes are usually coupled to the elongation and shortening of the microtubules to which they are bound. The length of kinetochore-associated MT changes by incorporation or loss of tubulin subunits, principally at their chromosome-bound ends (Hunt & McIntosh, 1998). The rapid transitions between polymerization and depolyme-O.S. Awotunde and K. Lechward contributed equally to this work

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