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Related Experiment Video

Updated: Jun 25, 2026

Investigating Tissue- and Organ-specific Phytochrome Responses using FACS-assisted Cell-type Specific Expression Profiling in Arabidopsis thaliana
10:10

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Published on: May 29, 2010

Partial characterization of oat and rye phytochrome.

H V Rice1, W R Briggs

  • 1The Biological Laboratories, Harvard University, Cambridge, Massachusetts 02138.

Plant Physiology
|May 1, 1973
PubMed
Summary
This summary is machine-generated.

Oat and rye phytochrome structural characteristics were analyzed. Rye phytochrome

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Area of Science:

  • Plant molecular biology
  • Protein biochemistry

Background:

  • Phytochromes are crucial plant photoreceptors.
  • Understanding phytochrome structure is key to elucidating light signaling pathways.

Purpose of the Study:

  • To characterize the structural properties of purified oat and rye phytochrome.
  • To compare the molecular weights, subunit composition, and amino acid profiles of oat and rye phytochrome.

Main Methods:

  • Analytical gel chromatography (Sephadex G-200)
  • Polyacrylamide gel electrophoresis (PAGE)
  • Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE)
  • N-terminal analysis
  • Amino acid analysis

Main Results:

  • Oat phytochrome: MW ~62,000 Da. Rye phytochrome: MW ~375,000 Da (nondenatured), ~120,000 Da (SDS-PAGE), suggesting a multimeric structure.
  • Amino acid analysis of rye phytochrome significantly differed from previous reports.
  • Oat phytochrome has four N-terminal residues; rye phytochrome has two.
  • Proteinolysis of rye phytochrome yielded a product resembling oat phytochrome.

Conclusions:

  • Rye phytochrome exhibits a multimeric structure, distinct from oat phytochrome.
  • The structural characteristics of purified rye phytochrome are likely representative of the native protein.
  • Discrepancies in amino acid analysis highlight the need for further investigation into rye phytochrome composition.