Binding Proteins to Phytochrome A in Etiolated Pea Seedlings

概要

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In order to detect and characterize a putative receptor(s) for a signal from PhyA, proteins that bind to purified pea PhyA were searched for in the crude extract of etiolated pea seedlings with affinity chromatography. PhyA was coupled to the column substrate either in P_R form (P_R column) or in red-irradiated form (P_<FR> column). The coupled PhyA of both columns retains its spectral reversibility between P_R and P_<FR> although their peptide mapping by trypsin digestion suggests that the C-terminal half of PhyA in the P_<FR> column is partially fixed in P_<FR> structure. 15 polypeptides were detected reproducibly in the elution from the P_<FR> column by silver-staining of SDS-PAGE. These 15 polypeptides may form two complexes judging from their elution profiles. Of the 15 polypeptides, the 6 major polypeptides have approximate mol wt of 80, 55, 53, 46, 40 and 35 kDa. On the other hand, only a trace amount of protein, which mainly consists of the 46 kDa species, was eluted from P_R column, indicating the presence of P_<FR>-specific BPs in the crude extract of etiolated pea seedlings. Of the 6 major polypeptides, the 40 kDa species binds to the PhyA in a photoreversible manner.
日本植物生理学会の論文