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

The Anatomy of Chloroplasts01:08

The Anatomy of Chloroplasts

5.4K
Green algae and plants, including green stems and unripe fruit, harbor specialized organelles called chloroplasts to carry out photosynthesis. They coordinate both stages of photosynthesis — the light-dependent reactions and the light-independent reactions. The light-dependent reactions use sunlight to release oxygen and produce chemical energy in the form of ATP and NADPH, and the light-independent reactions capture CO2 and use ATP and NADPH to produce sugar.
Structure of...
5.4K
Protein Transport to the Stroma01:24

Protein Transport to the Stroma

1.9K
Chloroplasts are triple membrane structures with an outer membrane, an inner membrane, and a thylakoid membrane, each containing distinct metabolite transporters, membrane translocons, and enzymes. Appropriate sorting and translocating these proteins to their correct membrane systems is essential for chloroplast function.
Protein complexes called the translocon of the outer chloroplast membrane or TOC complex, and the translocon of the inner chloroplast membrane or TIC complex mediate the...
1.9K
Anatomy of Chloroplasts01:07

Anatomy of Chloroplasts

111.1K
Green algae and plants, including green stems and unripe fruit, harbor chloroplasts—the vital organelles where photosynthesis takes place. In plants, the highest density of chloroplasts is found in the mesophyll cells of leaves.
111.1K
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
Photosystems01:32

Photosystems

5.0K
Photosystems are multiprotein complexes that form the functional units of photosynthesis in plants, algae, and cyanobacteria. They are found embedded in the membrane of tiny sac-like structures called thylakoids placed inside the chloroplast.
Functioning of Photosystems
Photosystems contain many pigment molecules, such as chlorophylls and carotenoids, arranged in a particular organization across two domains — the antenna complex and the reaction center. The main aim of the pigment...
5.0K

You might also read

Related Articles

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

Sort by
Same author

The secreted redox sensor roGFP2-Orp1 reveals oxidative dynamics in the plant apoplast.

Plant biology (Stuttgart, Germany)·2025
Same author

A modular high-throughput approach for advancing synthetic biology in the chloroplast of Chlamydomonas.

Nature plants·2025
Same author

Correction: Required minimal protein domain of flower for synaptobrevin2 endocytosis in cytotoxic T cells.

Cellular and molecular life sciences : CMLS·2025
Same author

A truncated variant of the ribosome-associated trigger factor specifically contributes to plant chloroplast ribosome biogenesis.

Nature communications·2025
Same author

Required minimal protein domain of flower for synaptobrevin2 endocytosis in cytotoxic T cells.

Cellular and molecular life sciences : CMLS·2024
Same author

The cyanobacterial protein VIPP1 forms ESCRT-III-like structures on lipid bilayers.

Nature structural & molecular biology·2024

Related Experiment Video

Updated: Aug 26, 2025

Purification of Active Photosystem I-Light Harvesting Complex I from Plant Tissues
07:10

Purification of Active Photosystem I-Light Harvesting Complex I from Plant Tissues

Published on: February 3, 2023

1.3K

Structural features of chloroplast trigger factor determined at 2.6 Å resolution.

Yvonne Carius1, Fabian Ries2, Karin Gries2

  • 1Department of Structural Biology, Saarland University, Center of Human and Molecular Biology (ZHMB), Faculty of Medicine, Building 60, 66421 Homburg, Germany.

Acta Crystallographica. Section D, Structural Biology
|October 3, 2022
PubMed
Summary

The crystal structure of Chlamydomonas reinhardtii trigger factor reveals a dragon-shaped conformation similar to bacterial forms. However, distinct charge distributions in its chaperone domain suggest specialized function in plant chloroplasts.

Keywords:
Chlamydomonas reinhardtiiPPIaseschaperone trigger factorchloroplastsco-translational foldingmolecular chaperones

More Related Videos

Studying the Supramolecular Organization of Photosynthetic Membranes within Freeze-fractured Leaf Tissues by Cryo-scanning Electron Microscopy
13:52

Studying the Supramolecular Organization of Photosynthetic Membranes within Freeze-fractured Leaf Tissues by Cryo-scanning Electron Microscopy

Published on: June 23, 2016

12.6K
A New Approach for the Comparative Analysis of Multiprotein Complexes Based on 15N Metabolic Labeling and Quantitative Mass Spectrometry
08:04

A New Approach for the Comparative Analysis of Multiprotein Complexes Based on 15N Metabolic Labeling and Quantitative Mass Spectrometry

Published on: March 13, 2014

12.3K

Related Experiment Videos

Last Updated: Aug 26, 2025

Purification of Active Photosystem I-Light Harvesting Complex I from Plant Tissues
07:10

Purification of Active Photosystem I-Light Harvesting Complex I from Plant Tissues

Published on: February 3, 2023

1.3K
Studying the Supramolecular Organization of Photosynthetic Membranes within Freeze-fractured Leaf Tissues by Cryo-scanning Electron Microscopy
13:52

Studying the Supramolecular Organization of Photosynthetic Membranes within Freeze-fractured Leaf Tissues by Cryo-scanning Electron Microscopy

Published on: June 23, 2016

12.6K
A New Approach for the Comparative Analysis of Multiprotein Complexes Based on 15N Metabolic Labeling and Quantitative Mass Spectrometry
08:04

A New Approach for the Comparative Analysis of Multiprotein Complexes Based on 15N Metabolic Labeling and Quantitative Mass Spectrometry

Published on: March 13, 2014

12.3K

Area of Science:

  • Molecular Biology
  • Structural Biology
  • Biochemistry

Background:

  • Protein folding is crucial and relies on molecular chaperones.
  • Trigger factor (TF) is a ribosome-associated chaperone found in prokaryotes and plant chloroplasts, binding nascent polypeptides.
  • Bacterial TF has a well-defined dragon-shaped structure with domains for ribosome binding, peptidyl-prolyl cis-trans isomerization (PPIase), and substrate interaction.

Purpose of the Study:

  • To determine the crystal structure of plastidic trigger factor from Chlamydomonas reinhardtii.
  • To investigate the molecular mechanism and structural adaptations of eukaryotic TF in plant organelles.
  • To compare the structure of eukaryotic TF with its bacterial orthologs.

Main Methods:

  • X-ray crystallography was used to determine the structure of Chlamydomonas reinhardtii plastidic trigger factor at 2.6 Å resolution.
  • A truncated protein lacking the N-terminal ribosome-binding domain was used due to high intramolecular flexibility.
  • Structural comparisons were made between the eukaryotic TF and bacterial TF.

Main Results:

  • The eukaryotic TF from C. reinhardtii adopts a dragon-shaped conformation, similar to bacterial TF.
  • The C-terminal chaperone domain exhibits altered charge distributions, modified helical arm positioning, and distinct substrate-binding surface characteristics.
  • The PPIase domain is structurally conserved but shows weak activity and an unusual orientation relative to the C-terminal domain.

Conclusions:

  • Chloroplast TF has diversified from bacterial TF, with structural adaptations in its chaperone domain.
  • These adaptations suggest specialized functional roles for eukaryotic TF within chloroplasts.
  • The findings provide insights into the evolution and function of ribosome-associated chaperones in different cellular compartments.