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Related Concept Videos

Vesicular Tubular Clusters01:45

Vesicular Tubular Clusters

After budding out from the ER membrane, some COPII vesicles lose their coat and fuse with one another to form larger vesicles and interconnected tubules called vesicular tubular clusters or VTCs. These clusters constitute a compartment at the ER-Golgi interface known as ERGIC (Endoplasmic Reticulum Golgi Intermediate Compartment). The ERGIC is a mobile membrane-bound cargo transport system that sorts proteins secreted from ER and delivers them to the Golgi.
With the help of motor proteins such...
SNAREs and Membrane Fusion01:43

SNAREs and Membrane Fusion

Once a transport vesicle has recognized its target organelle, the vesicular membrane needs to fuse with the target membrane to unload the cargo. Transmembrane proteins called SNAREs present on organelle membranes and their vesicles, mediate vesicle fusion.
SNAREs exist in pairs that symmetrically interact and catalyze the fusion of the lipid bilayers in vesicle and target organelle. v-SNARE in the vesicle membrane are single polypeptide chains that bind to a complementary t-SNARE, composed of 2...
Clathrin Coated Vesicles01:12

Clathrin Coated Vesicles

Clathrin-coated vesicles use endocytosis to transport receptors and lysosomal hydrolases from the Golgi to the lysosome in the late secretory pathway. Clathrin-mediated endocytosis was the first described endocytic process, and Clathrin-coated vesicles remain one of the most well-studied transport vesicles. The molecular machinery that generates clathrin-coated vesicles comprises over 50 proteins that precisely coordinate vesicle formation. Cell surface receptors concentrated in indented sites...
Pinching-off of Coated Vesicles01:32

Pinching-off of Coated Vesicles

Vesicle budding is orchestrated by distinct cytosolic proteins such as adaptor proteins, coat proteins, and GTPases. To initiate vesicle budding, membrane-bending proteins containing crescent-shaped BAR domains bind to the lipid heads in the bilayer and distort the membrane to form a protein-coated vesicle bud. Adaptors proteins such as AP2 for clathrin-coated vesicles can nucleate on the deformed membrane. Finally, coat proteins such as clathrin or COPI and COPII assemble into a coat forming...
Intralumenal Vesicles and Multivesicular Bodies01:38

Intralumenal Vesicles and Multivesicular Bodies

Intraluminal vesicles (ILVs) are small vesicles 50-80 nm in diameter formed during the maturation of early endosomes. A specialized endosome containing numerous ILVs is called a multivesicular body (MVB). ILVs contain internalized molecules such as antigens, nucleic acids, proteins, and metabolites. Some of these molecules are released from the MVBs inside exosomes and are transported to other cells. Other MVBs contain molecules that are retained in the ILVs and are later degraded within the...
Protein Complex Assembly02:41

Protein Complex Assembly

Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...

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Related Experiment Video

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In vitro Reconstitution of Cytoskeletal Networks inside Phase Separated Giant Unilamellar Vesicles (GUVs)
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Published on: June 20, 2025

[FeFe]-hydrogenase models assembled into vesicular structures.

Kristin Menzel1, Ulf-Peter Apfel, Nonio Wolter

  • 1Department of Pharmaceutical Technology, Friedrich-Schiller-University Jena , Jena , Germany .

Journal of Liposome Research
|September 7, 2013
PubMed
Summary

Researchers created nanoreactors by embedding iron-sulfur clusters within vesicles. These minimal cell models demonstrate catalytic activity, offering insights into the origin of life and potential for chemical synthesis.

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Area of Science:

  • Biochemistry
  • Origin of Life Studies
  • Nanotechnology

Background:

  • Compartmentalization is crucial for life's origin, as proposed by the Iron-Sulfur World hypothesis.
  • Autocatalytic inorganic redox systems involving iron and sulfur are considered precursors to complex organic molecule synthesis.

Purpose of the Study:

  • To develop functional nanoreactors mimicking early life conditions.
  • To investigate the incorporation and catalytic activity of modified hydrogenase models within vesicular systems.

Main Methods:

  • Covalent coupling of [FeFe]-hydrogenase models ([2Fe-2S] cluster) to oleic acid or polybutadiene-polyethyleneoxide (PB-PEO).
  • Incorporation of modified models into phospholipid liposomes or polymer-based polymersomes.
  • Characterization using spectrophotometric iron quantification, photon correlation spectroscopy (PCS), zeta potential, and cryo-transmission electron microscopy (Cryo-TEM).

Main Results:

  • Successful incorporation of modified hydrogenase models into liposomes (up to 3.15% molar proportion) and polymersomes (up to 28%).
  • Vesicular systems demonstrated catalytic activity for hydrogen generation within the intravesicular microenvironment.
  • The modified models function as nanoreactors within the vesicle bilayers.

Conclusions:

  • Vesicular systems incorporating modified [FeFe]-hydrogenase models serve as effective nanoreactors.
  • These systems can generate hydrogen for reducing encapsulated substances, acting as a minimal cell model.
  • The findings support the role of compartmentalization and inorganic catalysts in prebiotic chemistry and the origin of life.