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Isolation of phosphorylated and dephosphorylated forms of the CP43 internal antenna of photosystem II in Hordeum vulgare L.
Flora Andreucci, Roberto Barbato, Chiara Picollo and Anna Segalla
Journal of Experimental Botany
Vol. 56, No. 414 (April 2005), pp. 1239-1244
Published by: Oxford University Press
Stable URL: http://www.jstor.org/stable/24030921
Page Count: 6
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As a consequence of variation in environmental factors, light being the most important one, a number of photosystem II polypeptides may be reversibly phosphorylated by thylakoid-bound kinase(s). Among them, the reaction centre D1 and D2 polypeptides, the PsbH subunit, and the inner antenna CP43. Here, the separation of two forms of CP43 by high-resolution denaturing polyacrylamide gel electrophoresis is reported. By means of immunoblotting with antibody to phosphothreonine-containing proteins and authentic CP43 and limited proteolysis, these two bands could be identified as the phosphorylated and dephosphorylated forms of CP43. Using non-denaturing isoelectrofocusing, a chromatographically derived CP43-enriched fraction could be resolved into three different native forms of CP43. Among them, one was found to be a phosphorylated form, whereas the other two were dephosphorylated forms of the protein. With respect to other methods, the procedure described here allows the isolation, for the first time, of a fully homogeneous population of this chlorophyll–protein complex, opening the way to the study of the role of phopshorylation on functional properties of this core antenna protein.
Journal of Experimental Botany © 2005 Oxford University Press