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

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...

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Bibliographic Details
Published in:The Plant cell 1997-12, Vol.9 (12), p.2271-2280
Main Authors: Elich, T.D, Chory, J
Format: Article
Language:English
Subjects:
ABSORBANCE
ABSORBANCIA
Absorption spectra
Arabidopsis - chemistry
Arabidopsis - genetics
Arabidopsis - radiation effects
Arabidopsis Proteins
ARABIDOPSIS THALIANA
Base Sequence
Biochemistry
CHEMICAL REACTIONS
Chromophores
CRECIMIENTO
CROISSANCE
Darkness
DNA Primers - genetics
ESPECTROMETRIA
FAR RED LIGHT
FITOCROMA
Genes, Plant
GROWTH
HIPOCOTILOS
HYPOCOTYLE
HYPOCOTYLS
INDUCED MUTATION
LARGURA
LENGTH
LIGHT
LONGUEUR
LUMIERE
LUZ
Missense mutation
MUTACION INDUCIDA
MUTANT
MUTANTES
MUTANTS
Mutation
MUTATION PROVOQUEE
NONPHOTOCHEMICAL REVERSION
Oats
Phenotype
Phenotypes
Photochemistry
Photoreceptor Cells
PHYTOCHROME
Phytochrome - chemistry
Phytochrome - genetics
Phytochrome - radiation effects
Phytochrome B
Plant cells
Plants - genetics
Plants - metabolism
Plants - radiation effects
PLANTULAS
PLANTULE
REACCIONES QUIMICAS
REACTION CHIMIQUE
RED LIGHT
Saccharomyces cerevisiae - genetics
SEEDLINGS
Space life sciences
SPECTRAL DATA
SPECTROMETRIE
SPECTROMETRY
Spectrophotometry
Transcription Factors
Yeasts
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Description
Summary: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
ISSN:1040-4651
1532-298X
DOI:10.1105/tpc.9.12.2271