Journal Article

Binding Proteins to Phytochrome A in Etiolated Pea Seedlings

Takashi Shimada, Mitsue Miyao-Tokutomi and Satoru Tokutomi

in Plant and Cell Physiology

Published on behalf of Japanese Society of Plant Physiologists

Volume 40, issue 3, pages 281-288
Published in print January 1999 | ISSN: 0032-0781
Published online January 1999 | e-ISSN: 1471-9053 | DOI: http://dx.doi.org/10.1093/oxfordjournals.pcp.a029539
Binding Proteins to Phytochrome A in Etiolated Pea Seedlings

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  • Biochemistry
  • Molecular and Cell Biology
  • Plant Sciences and Forestry

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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 PR form (PR column) or in red-irradiated form (PFR column). The coupled PhyA of both columns retains its spectral reversibility between PR and PFR, although their peptide mapping by trypsin digestion suggests that the C-terminal half of PhyA in the PFR column is partially fixed in PFR structure. 15 polypeptides were detected reproducibly in the elution from the PFR 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 PR column, indicating the presence of PFR-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.

Keywords: Affinity chromatography; Binding protein; Phytochrome; Phototransformation; Pisum sativum; Signal transduction

Journal Article.  0 words. 

Subjects: Biochemistry ; Molecular and Cell Biology ; Plant Sciences and Forestry

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