BAIT

HFR1

FBI1, LONG HYPOCOTYL IN FAR-RED, REDUCED PHYTOCHROME SIGNALING 1, REDUCED SENSITIVITY TO FAR-RED LIGHT 1, REP1, RSF1, T6A9.4, T6A9_4, AT1G02340
transcription factor HFR1
Arabidopsis thaliana (Columbia)

Two-hybrid

Bait protein expressed as a DNA binding domain (DBD) fusion and prey expressed as a transcriptional activation domain (TAD) fusion and interaction measured by reporter gene activation.

Publication

Repression of light signaling by Arabidopsis SPA1 involves post-translational regulation of HFR1 protein accumulation.

Yang J, Lin R, Hoecker U, Liu B, Xu L, Wang H

Arabidopsis uses two major classes of photoreceptors to mediate seedling de-etiolation. The cryptochromes (cry1 and cry2) absorb blue/ultraviolet-A light, whereas the phytochromes (phyA-phyE) predominantly regulate responses to red/far-red light. Arabidopsis COP1 represses light signaling by acting as an E3 ubiquitin ligase in the nucleus, and is responsible for targeted degradation of a number of photomorphogenesis-promoting factors, including HY5, LAF1, phyA, ... [more]

Plant J. Jul. 01, 2005; 43(1);131-41 [Pubmed: 15960622]

Throughput

  • Low Throughput

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
HFR1 SPA1
Reconstituted Complex
Reconstituted Complex

An interaction is inferred between proteins in vitro. This can include proteins in recombinant form or proteins isolated directly from cells with recombinant or purified bait. For example, GST pull-down assays where a GST-tagged protein is first isolated and then used to fish interactors from cell lysates are considered reconstituted complexes (e.g. PUBMED: 14657240, Fig. 4A or PUBMED: 14761940, Fig. 5). This can also include gel-shifts, surface plasmon resonance, isothermal titration calorimetry (ITC) and bio-layer interferometry (BLI) experiments. The bait-hit directionality may not be clear for 2 interacting proteins. In these cases the directionality is up to the discretion of the curator.

Low-BioGRID
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Curated By

  • BioGRID