Binding proteins to phytochrome A in etiolated pea seedlings

Takashi Shimada, Mitsue Miyao-Tokutomi, Satoru Tokutomi

Research output: Contribution to journalArticlepeer-review


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.

Original languageEnglish
Pages (from-to)281-288
Number of pages8
JournalPlant and Cell Physiology
Issue number3
Publication statusPublished - 1999
Externally publishedYes


  • Affinity chromatography
  • Binding protein
  • Phototransformation
  • Phytochrome
  • Pisum sativum
  • Signal transduction

ASJC Scopus subject areas

  • Physiology
  • Plant Science
  • Cell Biology


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