Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Cell Signaling in Plants01:25

Cell Signaling in Plants

5.6K
Plant cells communicate to coordinate their cycle of growth, flowering and fruiting, and activities in roots, shoots, and leaves in response to the changing environmental conditions. Plant signaling is distinct from animal signaling. Plants primarily utilize enzyme-linked receptors, whereas the largest class of cell-surface receptors in animals are G-protein coupled receptors (GPCRs). Unlike animals, receptor tyrosine kinases are rare in plants. Instead, plants have a diverse class of...
5.6K
Photoreceptors and Plant Responses to Light02:00

Photoreceptors and Plant Responses to Light

20.3K
Light plays a significant role in regulating the growth and development of plants. In addition to providing energy for photosynthesis, light provides other important cues to regulate a range of developmental and physiological responses in plants.
20.3K
Biological Clocks and Seasonal Responses02:45

Biological Clocks and Seasonal Responses

34.6K
The circadian—or biological—clock is an intrinsic, timekeeping, molecular mechanism that allows plants to coordinate physiological activities over 24-hour cycles called circadian rhythms. Photoperiodism is a collective term for the biological responses of plants to variations in the relative lengths of dark and light periods. The period of light-exposure is called the photoperiod.
34.6K
Protein Transport to the Inner Chloroplast Membrane01:18

Protein Transport to the Inner Chloroplast Membrane

2.1K
Proteins targeted to the inner chloroplast membrane, or plastid proteins, are transported by two general pathways: the stop-transfer and the re-insertion or post-import pathways. Most plastid proteins carry N-terminal transit sequences and internal import sequences targeting it to the specific chloroplast subcompartment. Proteins targeted by the stop-transfer pathway have internal hydrophobic sequences that inhibit their translocation into the stroma. As a result, these precursors are arrested...
2.1K
Protein Transport to the Outer Chloroplast Membrane01:11

Protein Transport to the Outer Chloroplast Membrane

2.0K
Chloroplast outer membrane proteins encoded by the nucleus are synthesized in the cytosol. Soon after synthesis, they bind cytosolic factors such as 14-3-3 protein and the Hsp70 chaperones that keep these precursors in an unfolded state until their translocation.
Two models describe the mechanism of precursor recognition and entry across the outer membrane through the TOC complex. Model 1 suggests the newly synthesized precursor binds to the TOC receptor 159 and forms a complex.
2.0K
Plant Hormones01:56

Plant Hormones

24.0K
Plant hormones—or phytohormones—are chemical molecules that modulate one or more physiological processes of a plant. In animals, hormones are often produced in specific glands and circulated via the circulatory system. However, plants lack hormone-producing glands.
24.0K

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Cryo-electron microscopy structures of human cone visual pigments.

Science (New York, N.Y.)·2026
Same author

Ultrarapid MC1R protein and associated plumage color evolution in the domestic chicken.

Proceedings of the National Academy of Sciences of the United States of America·2026
Same author

Increased hydrogen and ethanol production in transformants of the filamentous cyanobacterium Phormidium lacuna.

Archives of microbiology·2026
Same author

A Cryptic Pocket Allosterically Modulates Oligosaccharide Binding to DC-SIGN.

JACS Au·2026
Same author

Proton-Coupled Chromophore and Protein Structural Changes Control Phytochrome Activation.

Biochemistry·2026
Same author

Photoisomerization of phytochrome's chromophore: a vibrational spectroscopic view on the primary ground state processes.

RSC advances·2025

Related Experiment Video

Updated: Jul 4, 2025

Luciferase Complementation Imaging Assay in Nicotiana benthamiana Leaves for Transiently Determining Protein-protein Interaction Dynamics
07:55

Luciferase Complementation Imaging Assay in Nicotiana benthamiana Leaves for Transiently Determining Protein-protein Interaction Dynamics

Published on: November 20, 2017

14.0K

Phytochrome-Interacting Proteins.

Gero Kaeser1, Norbert Krauß1, Clare Roughan1

  • 1Karlsruhe Institute of Technology (KIT), Joseph Gottlieb Kölreuter Institut für Pflanzenwissenschaften (JKIP), Fritz-Haber-Weg 4, D-76131 Karlsruhe, Germany.

Biomolecules
|January 26, 2024
PubMed
Summary
This summary is machine-generated.

Phytochromes are light-sensing proteins found in many organisms. This study explores their interacting partners, revealing insights into signal transduction pathways and using AI to model bacterial phytochrome interactions.

Keywords:
CryPIF3PKS2bacterialfungalinteractionplant

More Related Videos

Protein-protein Interactions Visualized by Bimolecular Fluorescence Complementation in Tobacco Protoplasts and Leaves
11:10

Protein-protein Interactions Visualized by Bimolecular Fluorescence Complementation in Tobacco Protoplasts and Leaves

Published on: March 9, 2014

21.0K
Investigating Tissue- and Organ-specific Phytochrome Responses using FACS-assisted Cell-type Specific Expression Profiling in Arabidopsis thaliana
10:10

Investigating Tissue- and Organ-specific Phytochrome Responses using FACS-assisted Cell-type Specific Expression Profiling in Arabidopsis thaliana

Published on: May 29, 2010

15.8K

Related Experiment Videos

Last Updated: Jul 4, 2025

Luciferase Complementation Imaging Assay in Nicotiana benthamiana Leaves for Transiently Determining Protein-protein Interaction Dynamics
07:55

Luciferase Complementation Imaging Assay in Nicotiana benthamiana Leaves for Transiently Determining Protein-protein Interaction Dynamics

Published on: November 20, 2017

14.0K
Protein-protein Interactions Visualized by Bimolecular Fluorescence Complementation in Tobacco Protoplasts and Leaves
11:10

Protein-protein Interactions Visualized by Bimolecular Fluorescence Complementation in Tobacco Protoplasts and Leaves

Published on: March 9, 2014

21.0K
Investigating Tissue- and Organ-specific Phytochrome Responses using FACS-assisted Cell-type Specific Expression Profiling in Arabidopsis thaliana
10:10

Investigating Tissue- and Organ-specific Phytochrome Responses using FACS-assisted Cell-type Specific Expression Profiling in Arabidopsis thaliana

Published on: May 29, 2010

15.8K

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Photobiology

Background:

  • Phytochromes are biliproteins that function as photoreceptors in plants, fungi, bacteria, and other organisms.
  • They reversibly switch between red light (Pr) and far-red light (Pfr) forms upon light absorption, triggering conformational changes.
  • While plant phytochrome interactions are well-studied, knowledge of interacting partners for bacterial and fungal phytochromes is limited.

Purpose of the Study:

  • To elucidate the known interacting partners of phytochromes, particularly in bacteria and fungi.
  • To understand the context of these interactions within signal transduction pathways.
  • To explore the potential of AI-based modeling for predicting and analyzing phytochrome-interacting protein structures.

Main Methods:

  • Literature review and data compilation on identified phytochrome interacting proteins.
  • Analysis of known signal transduction pathways involving phytochromes.
  • Application of artificial intelligence (AI) system-based modeling software to predict and visualize interactions of bacterial phytochromes with their partners.

Main Results:

  • Identification and description of various phytochrome interacting proteins across different organisms.
  • Characterization of the roles of these interactions in signal transduction, nuclear translocation, and protein degradation.
  • Generation of predicted and modulated 3D models illustrating interactions between bacterial phytochromes and their partners.

Conclusions:

  • The study provides a comprehensive overview of phytochrome interacting partners and their functional significance.
  • AI-based modeling offers a promising approach to investigate the structural basis of phytochrome interactions, especially where experimental data is scarce.
  • Further research is needed to fully resolve the 3D structures and dynamics of these protein-protein interactions in various signaling contexts.