Evidence map›Paper›PMID 18715961›Full record

ArticlePlant physiology2008

Discrete and essential roles of the multiple domains of Arabidopsis FHY3 in mediating phytochrome A signal transduction.

Rongcheng Lin, Yibo Teng, Hee-Jin Park, Lei Ding, Christopher Black, Ping Fang, Haiyang Wang

Open access · hybridAbstract read
In one paragraph

Article in Plant physiology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
3.0field-weighted citation impact, top 9% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

32 citing papers in PubMed, 54 citations in OpenAlex.

  1. ThePlants (Basel, Switzerland) · 2026
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  2. Genome-Wide Analysis ofInternational journal of molecular sciences · 2026
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  9. Identification of genetic loci associated with five agronomic traits in alfalfa using multi-environment trials.TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik · 2023
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors at 2 institutions in 2 countries.

Rongcheng LinBoyce Thompson Institute for Plant Research, Cornell University, Ithaca, NY 14853, USA.
Yibo Teng
Hee-Jin Park
Lei Ding
Christopher Black
Ping Fang
Haiyang Wang
Zhejiang University · CNCornell University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Phytochrome A is the primary photoreceptor for mediating various far-red light-induced responses in higher plants. We recently showed that Arabidopsis (Arabidopsis thaliana) FAR-RED ELONGATED HYPOCOTYL3 (FHY3) and FAR-RED-IMPAIRED RESPONSE1 (FAR1), a pair of homologous proteins sharing significant sequence homology to Mutator-like transposases, act as novel transcription factors essential for activating the expression of FHY1 and FHL (for FHY1-like), whose products are required for light-induced phytochrome A nuclear accumulation and subsequent light responses. FHY3, FAR1, and Mutator-like transposases also share a similar domain structure, including an N-terminal C2H2 zinc finger domain, a central putative core transposase domain, and a C-terminal SWIM motif (named after SWI2/SNF and MuDR transposases). In this study, we performed a promoter-swapping analysis of FHY3 and FAR1. Our results suggest that the partially overlapping functions of FHY3 and FAR1 entail divergence of their promoter activities and protein subfunctionalization. To gain a better understanding of the molecular mode of FHY3 function, we performed a structure-function analysis, using site-directed mutagenesis and transgenic approaches. We show that the conserved N-terminal C2H2 zinc finger domain is essential for direct DNA binding and biological function of FHY3 in mediating light signaling, whereas the central core transposase domain and C-terminal SWIM domain are essential for the transcriptional regulatory activity of FHY3 and its homodimerization or heterodimerization with FAR1. Furthermore, the ability to form homodimers or heterodimers largely correlates with the transcriptional regulatory activity of FHY3 in plant cells. Together, our results reveal discrete roles of the multiple domains of FHY3 and provide functional support for the proposition that FHY3 and FAR1 represent transcription factors derived from a Mutator-like transposase(s).

Indexed as

Signal TransductionAmino Acid SequenceArabidopsisArabidopsis ProteinsGene Expression Regulation, PlantGenes, PlantLightMolecular Sequence DataMutagenesis, Site-DirectedNuclear ProteinsPhytochromePhytochrome APlants, Genetically ModifiedPlasmidsPromoter Regions, GeneticRNA, PlantArabidopsis ProteinsFAR1 protein, ArabidopsisFHY3 protein, ArabidopsisNuclear ProteinsPhytochromePhytochrome ARNA, PlantTranscription Factors

Identifiers

PMID18715961
PMCPMC2556831
OpenAlexW2005577765

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.