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Biochemical characterization of Arabidopsis wild-type and mutant phytochrome B holoproteins

Academic Article
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Overview

authors

  • Elich, T. D.
  • Chory, Joanne

publication date

  • December 1997

journal

  • Plant Cell  Journal

abstract

  • Although phytochrome B (phyB) plays a particularly important role throughout the life cycle of a plant, it has not been studied in detail at the molecular level due to its low abundance. Here, we report on the expression, assembly with chromophore, and purification of epitope-tagged Arabidopsis phyB. In addition, we have reconstructed two missense mutations, phyB-4 and phyB-101, isolated in long hypocotyl screens. We show that mutant proteins phyB-4 and phyB-101 exhibit altered spectrophotometric and biochemical properties relative to the wild-type protein. In particular, we demonstrate that phyB-101 Pfr exhibits rapid nonphotochemical (dark) reversion to Pr that results in a lower photoequilibrium level of the active Pfr form. We conclude that this occurs in vivo as well because phyB-101 mutants are shown to lack an end-of-day-far-red hypocotyl elongation response that requires a stable Pfr species. We propose that this Pfr instability may be the primary molecular mechanism underlying the phyB-101 mutant phenotype.

subject areas

  • Arabidopsis
  • Arabidopsis Proteins
  • Base Sequence
  • DNA Primers
  • Darkness
  • Genes, Plant
  • Mutation
  • Phenotype
  • Photochemistry
  • Photoreceptor Cells
  • Phytochrome
  • Phytochrome B
  • Plants
  • Saccharomyces cerevisiae
  • Spectrophotometry
  • Transcription Factors
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Identity

PubMed Central ID

  • PMC157073

International Standard Serial Number (ISSN)

  • 1040-4651

Digital Object Identifier (DOI)

  • 10.1105/tpc.9.12.2271

PubMed ID

  • 9437866
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Additional Document Info

start page

  • 2271

end page

  • 2280

volume

  • 9

issue

  • 12

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