Light-regulated nuclear import and degradation of arabidopsis phytochrome-a N-terminal fragments

Iris Wolf, Stefan Kircher, Erzsébet Fejes, L. Kozma-Bognár, Eberhard Schäfer, Ferenc Nagy, E. Ádám

Research output: Contribution to journalArticle

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Abstract

The photoreceptor phytochrome-A (phyA) regulates germination and seedling establishment by mediating very low fluence (VLFR) and far-red high irradiance (FR-HIR) responses in Arabidopsis thaliana. In darkness, phyA homodimers exist in the biologically inactive Pr form and are localized in the cytoplasm. Light induces formation of the biologically active Pfr form and subsequent rapid nuclear import. PhyA Pfr, in contrast to the Pr form, is labile and has a half-life of ∼30 min. We produced transgenic plants in a phyA-201 null background that express the PHYA-yellow fluorescent protein (YFP) or the PHYA686-YFP-dimerization domain (DD) and PHYA686-YFP-DD-nuclear localization signal (NLS) or PHYA686-YFP-DD-nuclear exclusion signal (NES) fusion proteins. The PHYA686-YFP fusion proteins contained the N-terminal domain of phyA (686 amino acid residues), a short DD and the YFP. Here we report that (i) PHYA686-YFP-DD fusion protein is imported into the nucleus in a light-dependent fashion; (ii) neither of the PHYA686 fusion proteins is functional in FR-HIR and nuclear VLFR; and (iii) the phyA-dependent, blue light-induced inhibition of hypocotyl growth is mediated by the PHYA686-YFP-DD-NES but not by the PHYA686-YFP-DD-NLS and PHYA686-YFP-DD fusion proteins. We demonstrate that (i) light induces degradation of all PHYA N-terminal-containing fusion proteins and (ii) these N-terminal domain-containing fusion proteins including the constitutively nuclear PHYA686-YFP-DD-NLS and predominantly cytoplasmic PHYA686-YFP-DD-NES degrade at comparable rates but markedly more slowly than PHYA-YFP, whereas (iii) light-induced degradation of the native phyA is faster compared with PHYA-YFP.

Original languageEnglish
Pages (from-to)361-372
Number of pages12
JournalPlant and Cell Physiology
Volume52
Issue number2
DOIs
Publication statusPublished - Feb 2011

Fingerprint

Phytochrome
Cell Nucleus Active Transport
Protein Multimerization
phytochrome
Arabidopsis
imports
dimerization
Phytochrome A
Light
degradation
Proteins
Nuclear Localization Signals
nuclear localization signals
nuclear yellow
proteins
yellow fluorescent protein
Protein Domains
Hypocotyl
Genetically Modified Plants
Darkness

Keywords

  • High irradiation response
  • Light-induced degradation
  • Nuclear import
  • Phytochrome-A
  • Signaling
  • Very low fluence response

ASJC Scopus subject areas

  • Plant Science
  • Physiology
  • Cell Biology

Cite this

Light-regulated nuclear import and degradation of arabidopsis phytochrome-a N-terminal fragments. / Wolf, Iris; Kircher, Stefan; Fejes, Erzsébet; Kozma-Bognár, L.; Schäfer, Eberhard; Nagy, Ferenc; Ádám, E.

In: Plant and Cell Physiology, Vol. 52, No. 2, 02.2011, p. 361-372.

Research output: Contribution to journalArticle

Wolf, Iris ; Kircher, Stefan ; Fejes, Erzsébet ; Kozma-Bognár, L. ; Schäfer, Eberhard ; Nagy, Ferenc ; Ádám, E. / Light-regulated nuclear import and degradation of arabidopsis phytochrome-a N-terminal fragments. In: Plant and Cell Physiology. 2011 ; Vol. 52, No. 2. pp. 361-372.
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AU - Schäfer, Eberhard

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