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Plant J. 2000 Feb;21(4):387-91.

Reversible binding of the starch-related R1 protein to the surface of transitory starch granules.

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Institut für Biochemie und Molekulare Physiologie, Universität Potsdam, Karl-Liebknecht-Str. 24-25, Haus 20, D-14476 Golm, Germany.


Intact starch granules were isolated from leaves of Solanum tuberosum L. (and from Pisum sativum L.), and the patterns of starch-associated proteins were determined by SDS-PAGE. Depending on the pretreatment of the leaves the protein patterns varied: a 160 kDa compound was present in the starch-associated protein fraction when the leaves were darkened and performed net starch degradation. However, following illumination (i.e. during net starch biosynthesis) the 160 kDa protein was recovered almost exclusively in a soluble state. The 160 kDa protein was identified to be the recently described starch-related R1 protein. In in vitro assays recombinant R1 did bind to starch granules isolated from either illuminated or darkened leaves. However, binding to the latter was more effective. It is concluded that, depending upon the metabolic state of the cells, the starch granule surface changes and thereby affects binding of the R1 protein.

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