Decoding of light signals by plant phytochromes and their interacting proteins.

  title={Decoding of light signals by plant phytochromes and their interacting proteins.},
  author={Gabyong Bae and Giltsu Choi},
  journal={Annual review of plant biology},
Phytochromes are red/far-red light photoreceptors that convert the information contained in external light into biological signals. The decoding process starts with the perception of red light, which occurs through photoisomerization of a chromophore located within the phytochrome, leading to structural changes that include the disruption of intramolecular interactions between the N- and C-terminal domains of the phytochrome. This disruption exposes surfaces required for interactions with other… 

Figures from this paper

Mapping light-driven conformational changes within the photosensory module of plant phytochrome B

Information is provided about structural changes occurring during photoconversion within phytochrome B and possible interaction sites for its N-terminal extension (NTE) utilising hydrogen/deuterium exchange rate analyses of its amide backbone and the newly identified light-dependency of two regions in the NTE.

Phytochrome Signaling Mechanisms

Phytochromes are red (R)/far-red (FR) light photoreceptors that play fundamental roles in photoperception of the light environment and the subsequent adaptation of plant growth and development. There

Rapid Examination of Phytochrome-Phytochrome Interacting Factor (PIF) Interaction by In Vitro Coimmunoprecipitation Assay.

  • I. PaikE. Huq
  • Biology, Environmental Science
    Methods in molecular biology
  • 2019
In this chapter, a protocol for rapid and simple light dependent in vitro coimmunoprecipitation betweenphytochromes and phytochrome interacting factors is described and can be adapted for other putative phy tochrome interacting proteins.

Plant Light Signaling Mediated by Phytochrome Photoreceptors

Several key components in the phytochrome-mediated light signaling have been identified from extensive research over several decades, which includes phy tochrome-interacting factor (PIF), constitutively photomorphogenic 1 (COP1), suppressor of phyA-105 (SPA), and elongated hypocotyl 5 (HY5).

Phytochrome: structural basis for its functions.

  • A. Nagatani
  • Environmental Science
    Current opinion in plant biology
  • 2010

An overview of phytochrome: An important light switch and photo-sensory antenna for regulation of vital functioning of plants

This review will focus on the importance of phytochromes, their mechanism of action and their application as an emerging field in plant biology.

Light-induced structural changes in a monomeric bacteriophytochrome

It is concluded that a monomer of the phytochrome photosensory core is sufficient to perform the light-induced structural changes, which implies that allosteric cooperation with the other monomer is not needed for structural activation.

Photoactivated phytochromes interact with HEMERA and promote its accumulation to establish photomorphogenesis in Arabidopsis.

It is shown that phytochromes directly interact with HMR to promote HMR protein accumulation in the light and mediates the formation of photobodies and the degradation of PIFs to establish photomorphogenesis.

Phytochrome-interacting factors have both shared and distinct biological roles

Compared recently published genome-wide ChIP data, developmental gene expression maps, and responses to various stimuli for the various PIFs, it is proposed that the biological roles of Pifs stem from their shared and distinct DNA binding targets and specific gene expression patterns.

Bacterial photosensory proteins: Regulatory functions and optogenetic applications

Three classes of light-sensory regulatory proteins, which have been identified in genomes of numerous phototrophic and nonphotosynthetic bacteria, are discussed: the UVA/blue light sensitive BLUF and



Degradation of phytochrome interacting factor 3 in phytochrome-mediated light signaling.

It is demonstrated that PIF3 is polyubiquitinated rapidly and subsequently degraded in PHYA and PHYB-mediated light signaling and that the degradation of Pif3 is mediated by the 26S proteasome.

Phytochrome structure and signaling mechanisms.

The discovery of new bacterial and cyanobacterial members of the phytochrome family within the last decade has greatly aided biochemical and structural characterization of this family, with the first crystal structure of a bacteriophytochrome photosensory core appearing in 2005.

Binding of phytochrome B to its nuclear signalling partner PIF3 is reversibly induced by light

It is concluded that photosensory signalling by phytochrome B involves light-induced, conformer-specific recognition of the putative transcriptional regulator PIF3, providing a potential mechanism for direct photoregulation of gene expression.

Dimers of the N-terminal domain of phytochrome B are functional in the nucleus

Findings indicate that the C-terminal domain of Arabidopsis phytochrome B attenuates the activity of phyB rather than positively transducing the signal.

Nucleo-cytoplasmic partitioning of the plant photoreceptors phytochromes.

The correlations found between the nuclear import of phytochromes (phyA and phyB) and various physiological responses regulated by these photoreceptors provides strong support for the hypothesis that light-quality and light-quantity dependent nuclear import is a major regulatory step at the cellular level.

A light-sensing knot revealed by the structure of the chromophore-binding domain of phytochrome

The structure provides the first three-dimensional glimpse into the photochromic behaviour of these photoreceptors and helps to explain the evolution of higher plant phytochromes from prokaryotic precursors.

Nuclear localization activity of phytochrome B.

Nuclear localization of phyB was suggested to be light-dependent and a substantial fraction of total phYB was recovered in the isolated nuclei, which suggests that the nuclear localization signal of the fragment is functional.

A cyanobacterial phytochrome two-component light sensory system.

The biliprotein phytochrome regulates plant growth and developmental responses to the ambient light environment through an unknown mechanism and is an ancient molecule that evolved from a more compact light sensor in cyanobacteria.

Phytochrome A is an irradiance-dependent red light sensor.

The discovery that phyA can function as an effective irradiance sensor, even in light environments that establish a high Pfr concentration, raises the possibility thatphyA may contribute significantly to the regulation of growth and development in daylight-grown plants.