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Related Concept Videos

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 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 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...
Protein Translocation Machinery on the ER Membrane01:28

Protein Translocation Machinery on the ER Membrane

The translocon complex situated on the ER membrane is the main gateway for the protein secretory pathway. It facilitates the transport of nascent peptides into the ER lumen and their insertion into the ER membrane.
Sec61 protein conducting channel
In eukaryotes, the translocon complex comprises a core heterotrimeric translocator channel called the Sec61 complex. This channel includes three transmembrane proteins, Sec61α, Sec61β, and Sec61γ, and is the largest subunit of the translocon complex.
Cotranslational Protein Translocation01:20

Cotranslational Protein Translocation

Translocation of proteins across membranes is an ancient process that occurs even in bacteria and archaebacteria. In fact, the components of the translocation machinery are still conserved between prokaryotes and eukaryotes.
Sec61 channel partners for cotranslational translocation
During cotranslational translocation, the Sec61 channel partners with the signal recognition particle (SRP), the signal recognition particle receptor (SR), and the ribosomes to transport the nascent polypeptide chain...
Bacterial Translocation and Protein Secretion01:26

Bacterial Translocation and Protein Secretion

Bacterial protein secretion involves translocation systems to ensure proteins reach their designated locations, including the plasma membrane, periplasm, outer membrane, or the external environment. These translocation systems are vital for bacterial physiology, supporting processes like membrane assembly, enzymatic activity in the periplasm, and interactions with the external environment. The division of labor between Sec and Tat pathways ensures efficiency in handling proteins with diverse...

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Related Experiment Video

Updated: Jun 7, 2026

Isolation of Physiologically Active Thylakoids and Their Use in Energy-Dependent Protein Transport Assays
12:25

Isolation of Physiologically Active Thylakoids and Their Use in Energy-Dependent Protein Transport Assays

Published on: September 28, 2018

Plastids contain a second sec translocase system with essential functions.

Courtney A Skalitzky1, Jonathan R Martin, Jessica H Harwood

  • 1Department of Botany, University of Wisconsin, Madison, Wisconsin 53706-1381, USA.

Plant Physiology
|November 6, 2010
PubMed
Summary

Researchers discovered two distinct Sec systems in plastids. One system, SCY1, is vital for thylakoid protein targeting, while the newly identified SCY2 system targets proteins to the inner envelope membrane.

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Last Updated: Jun 7, 2026

Isolation of Physiologically Active Thylakoids and Their Use in Energy-Dependent Protein Transport Assays
12:25

Isolation of Physiologically Active Thylakoids and Their Use in Energy-Dependent Protein Transport Assays

Published on: September 28, 2018

Identification of Plasmodesmal Localization Sequences in Proteins In Planta
08:07

Identification of Plasmodesmal Localization Sequences in Proteins In Planta

Published on: August 15, 2017

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 Biology
  • Cell Biology
  • Molecular Biology

Background:

  • Proteins synthesized in the cytoplasm but functioning in plastids require import and precise targeting.
  • While thylakoid targeting systems are known, the mechanism for inner envelope membrane protein integration from the stroma remained undescribed.

Purpose of the Study:

  • To identify and characterize the systems responsible for targeting proteins to specific plastid locations, particularly the inner envelope membrane.
  • To elucidate the distinct functions of different Sec systems within plastids.

Main Methods:

  • Genetic analysis using loss-of-function mutations in Arabidopsis thaliana.
  • Localization studies including chloroplast import assays, fractionation, and immunogold labeling.
  • Promoter-swap experiments to assess functional redundancy.

Main Results:

  • Two distinct Sec systems (SCY1 and SCY2) with non-redundant functions were identified in plastids.
  • Mutations in the SCY1 system (SCY1, SECA1, SECE1) led to albino seedlings and altered growth.
  • Mutations in the SCY2 system (SCY2, SECA2) caused embryo lethality, and SCY2 was localized to the envelope membrane.

Conclusions:

  • SCY1 and its components are involved in thylakoid protein targeting.
  • SCY2 and SECA2 constitute a novel envelope-localized Sec system essential for inner envelope membrane protein integration and translocation.
  • This discovery reveals a new pathway for protein targeting within plastids.