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Phytochrome and protein phosphorylation.

B R Singh1, P S Song

  • 1Food Research Institute, University of Wisconsin, Madison 53706.

Photochemistry and Photobiology
|July 1, 1990
PubMed
Summary
This summary is machine-generated.

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The active form of phytochrome (Pfr) may trigger plant signal transduction by altering protein phosphorylation. Its exposed chromophore may inhibit protein kinases, initiating a signaling cascade.

Area of Science:

  • Plant molecular biology
  • Photobiology
  • Signal transduction

Background:

  • The molecular mechanism of phytochrome-mediated signal transduction remains largely unknown.
  • The active Pfr form of phytochrome exposes its tetrapyrrole chromophore, unlike the Pr form.
  • Phytochrome's Pfr form is implicated in affecting cellular protein phosphorylation.

Purpose of the Study:

  • To review existing literature on phytochrome-mediated protein phosphorylation.
  • To investigate the role of phytochrome's chromophore topography in signal transduction.
  • To explore the hypothesis that Pfr inhibits protein kinase activity.

Main Methods:

  • Literature review focusing on phytochrome and protein phosphorylation.
  • Analysis of chromophore exposure in phytochrome's active Pfr form.

Related Experiment Videos

  • Examination of phosphorylation inhibition assays and protein kinase inhibition by tetrapyrroles.

    • Main Results:

    • Phytochrome's Pfr form's exposed chromophore is a key structural feature.
    • Evidence suggests Pfr may interact with cellular protein kinases.
    • Tetrapyrroles, in general, are known to inhibit protein kinase activity.

    Conclusions:

    • Phytochrome's Pfr form may initiate signal transduction by inhibiting protein kinase activity.
    • This inhibition could trigger a dephosphorylation-phosphorylation cascade.
    • Chromophore topography plays a potential role in phytochrome's signaling function.