PMID- 21969386
OWN - NLM
STAT- MEDLINE
DCOM- 20120710
LR  - 20211020
IS  - 1532-2548 (Electronic)
IS  - 0032-0889 (Print)
IS  - 0032-0889 (Linking)
VI  - 158
IP  - 1
DP  - 2012 Jan
TI  - Missense mutation in the amino terminus of phytochrome A disrupts the nuclear 
      import of the photoreceptor.
PG  - 107-18
LID - 10.1104/pp.111.186288 [doi]
AB  - Phytochromes are the red/far-red photoreceptors in higher plants. Among them, 
      phytochrome A (PHYA) is responsible for the far-red high-irradiance response and 
      for the perception of very low amounts of light, initiating the very-low-fluence 
      response. Here, we report a detailed physiological and molecular characterization 
      of the phyA-5 mutant of Arabidopsis (Arabidopsis thaliana), which displays 
      hyposensitivity to continuous low-intensity far-red light and shows reduced 
      very-low-fluence response and high-irradiance response. Red light-induced 
      degradation of the mutant phyA-5 protein appears to be normal, yet higher 
      residual amounts of phyA-5 are detected in seedlings grown under low-intensity 
      far-red light. We show that (1) the phyA-5 mutant harbors a new missense mutation 
      in the PHYA amino-terminal extension domain and that (2) the complex phenotype of 
      the mutant is caused by reduced nuclear import of phyA-5 under low fluences of 
      far-red light. We also demonstrate that impaired nuclear import of phyA-5 is 
      brought about by weakened binding affinity of the mutant photoreceptor to nuclear 
      import facilitators FHY1 (for FAR-RED ELONGATED HYPOCOTYL1) and FHL (for 
      FHY1-LIKE). Finally, we provide evidence that the signaling and degradation 
      kinetics of constitutively nuclear-localized phyA-5 and phyA are identical. Taken 
      together, our data show that aberrant nucleo/cytoplasmic distribution impairs 
      light-induced degradation of this photoreceptor and that the amino-terminal 
      extension domain mediates the formation of the FHY1/FHL/PHYA far-red-absorbing 
      form complex, whereby it plays a role in regulating the nuclear import of phyA.
FAU - Sokolova, Vladyslava
AU  - Sokolova V
AD  - Institute of Plant Biology, Biological Research Centre of the Hungarian Academy 
      of Sciences, H-6701 Szeged, Hungary.
FAU - Bindics, Janos
AU  - Bindics J
FAU - Kircher, Stefan
AU  - Kircher S
FAU - Adam, Eva
AU  - Adam E
FAU - Schafer, Eberhard
AU  - Schafer E
FAU - Nagy, Ferenc
AU  - Nagy F
FAU - Viczian, Andras
AU  - Viczian A
LA  - eng
GR  - Howard Hughes Medical Institute/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20111010
PL  - United States
TA  - Plant Physiol
JT  - Plant physiology
JID - 0401224
RN  - 0 (Arabidopsis Proteins)
RN  - 0 (FHL protein, Arabidopsis)
RN  - 0 (FHY1 protein, Arabidopsis)
RN  - 0 (PHYA protein, Arabidopsis)
RN  - 0 (Photoreceptors, Plant)
RN  - 0 (Phytochrome A)
RN  - 0 (Transcription Factors)
RN  - 11121-56-5 (Phytochrome)
SB  - IM
MH  - Active Transport, Cell Nucleus/*genetics
MH  - Arabidopsis/physiology
MH  - Arabidopsis Proteins/*genetics/metabolism
MH  - Cell Nucleus/genetics/metabolism
MH  - Light
MH  - *Mutation, Missense
MH  - Photoreceptors, Plant/metabolism
MH  - Phytochrome/genetics/metabolism
MH  - Phytochrome A/*genetics/*metabolism
MH  - Plants, Genetically Modified
MH  - Protein Stability
MH  - Protein Structure, Tertiary
MH  - Seedlings/genetics/growth & development
MH  - Signal Transduction
MH  - Transcription Factors/genetics/metabolism
MH  - Two-Hybrid System Techniques
PMC - PMC3252074
EDAT- 2011/10/05 06:00
MHDA- 2012/07/11 06:00
PMCR- 2013/01/01
CRDT- 2011/10/05 06:00
PHST- 2011/10/05 06:00 [entrez]
PHST- 2011/10/05 06:00 [pubmed]
PHST- 2012/07/11 06:00 [medline]
PHST- 2013/01/01 00:00 [pmc-release]
AID - pp.111.186288 [pii]
AID - 186288 [pii]
AID - 10.1104/pp.111.186288 [doi]
PST - ppublish
SO  - Plant Physiol. 2012 Jan;158(1):107-18. doi: 10.1104/pp.111.186288. Epub 2011 Oct 
      10.