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Related Concept Videos

Protein Transport to the Outer Chloroplast Membrane01:11

Protein Transport to the Outer Chloroplast Membrane

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.
Protein Transport to the Stroma01:24

Protein Transport to the Stroma

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...
Protein Transport to the Inner Chloroplast Membrane01:18

Protein Transport to the Inner Chloroplast Membrane

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...
Protein Transport to the Thylakoids01:22

Protein Transport to the Thylakoids

Thylakoids are membrane-bound sac-like structures within the chloroplast that serve as sites for photosynthesis. Thylakoid lumen contains many electron transport proteins and is enclosed by a thylakoid membrane rich in the light-harvesting complex. Proteins targeted to the thylakoids are transported as precursors and are sorted by the general TOC/TIC import pathway. Once the precursor reaches the stroma, stromal processing peptidases remove their transit signal and expose thylakoid signal...
Translocation of Proteins into the Mitochondria01:19

Translocation of Proteins into the Mitochondria

Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
Sorting of outer membrane proteins:
Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...
Toxoplasmosis01:28

Toxoplasmosis

Toxoplasmosis, a zoonotic disease caused by the protozoan Toxoplasma gondii, poses significant public health challenges globally due to its high seroprevalence and varied clinical manifestations. As an obligate intracellular parasite, T. gondii can infect all warm-blooded vertebrates, but felids are its only definitive hosts, shedding unsporulated oocysts into the environment. Humans typically acquire the infection through ingestion of tissue cysts in undercooked meat or oocysts from...

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Related Experiment Video

Updated: Jul 16, 2026

Affinity Purification of Chloroplast Translocon Protein Complexes Using the TAP Tag
07:01

Affinity Purification of Chloroplast Translocon Protein Complexes Using the TAP Tag

Published on: November 1, 2018

Ptr ToxA interacts with a chloroplast-localized protein.

Viola A Manning1, Linda K Hardison, Lynda M Ciuffetti

  • 1Department of Botany and Plant Pathology, Oregon State University, Corvallis 97331, USA.

Molecular Plant-Microbe Interactions : MPMI
|February 23, 2007
PubMed
Summary

Pyrenophora tritici-repentis toxin A (ToxA) targets chloroplasts in wheat. This study identifies ToxA binding protein 1 (ToxABP1) as a key interaction partner within chloroplasts, crucial for understanding tan spot disease.

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Studying Protein Import into Chloroplasts Using Protoplasts
06:29

Studying Protein Import into Chloroplasts Using Protoplasts

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Last Updated: Jul 16, 2026

Affinity Purification of Chloroplast Translocon Protein Complexes Using the TAP Tag
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Published on: November 1, 2018

Protein-protein Interactions Visualized by Bimolecular Fluorescence Complementation in Tobacco Protoplasts and Leaves
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Studying Protein Import into Chloroplasts Using Protoplasts
06:29

Studying Protein Import into Chloroplasts Using Protoplasts

Published on: December 10, 2018

Area of Science:

  • Plant pathology
  • Molecular biology
  • Biochemistry

Background:

  • Tan spot, caused by Pyrenophora tritici-repentis, is a significant wheat disease.
  • Host-selective toxins, like Ptr ToxA (ToxA), are critical virulence factors.
  • ToxA is known to enter wheat mesophyll cells and localize to chloroplasts in susceptible cultivars.

Purpose of the Study:

  • To identify plant proteins that interact with the wheat tan spot toxin, ToxA.
  • To elucidate the molecular mechanisms underlying ToxA pathogenicity in wheat.

Main Methods:

  • Yeast two-hybrid screening was employed to identify ToxA interacting proteins.
  • ToxABP1 localization and expression were analyzed in wheat cultivars.

Main Results:

  • ToxA interacts with a novel chloroplast protein, ToxA binding protein 1 (ToxABP1).
  • ToxABP1 shares structural similarities with animal endocytosis proteins.
  • ToxABP1 is present in chloroplast membranes and stroma in both sensitive and insensitive wheat, and ToxA interacts with a ToxABP1 complex on the chloroplast membrane.

Conclusions:

  • ToxABP1 is a plant protein that interacts with ToxA within chloroplasts.
  • This interaction may be a key step in ToxA-mediated pathogenesis of tan spot disease in wheat.
  • Understanding the ToxA-ToxABP1 interaction can inform strategies for disease resistance.