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

Coat Assembly and GTPases01:33

Coat Assembly and GTPases

3.6K
Vesicles incorporate different coat protein subunits in different cell locations, which changes the properties of the coat, such as the shape and geometry of the transport vesicles. Thus, vesicle coat proteins also play a significant role in cargo selection.
Coat assembly depends on the local availability of phosphatidylinositol phosphates or PIPs and GTP-binding proteins. Adaptor proteins, which link the coat proteins to the membrane, bind to these PIPs and play a crucial role in controlling...
3.6K
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

1.9K
1.9K
Fluid Mosaic Model01:19

Fluid Mosaic Model

13.1K
Scientists identified the plasma membrane in the 1890s and its principal chemical components (lipids and proteins) by 1915. The model for plasma membrane structure, proposed in 1935 by Hugh Davson and James Danielli, was the first model to be widely accepted in the scientific community. The model was based on the plasma membrane's "railroad track" appearance in early electron micrographs. Davson and Danielli theorized that the plasma membrane's structure resembled a sandwich...
13.1K
Protein Complex Assembly02:41

Protein Complex Assembly

11.1K
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...
11.1K
Mechanisms of Membrane Domain Formation00:59

Mechanisms of Membrane Domain Formation

3.2K
Different physical properties of lipids and proteins allow them to localize and form distinct islands or domains in the membrane. Some membrane domains are formed due to protein-protein interactions, whereas others are formed due to the presence of specific lipids such as sphingolipids and sterols—for example, large proteins, such as bacteriorhodopsin, aggregate and create distinct domains.
Another mechanism for membrane domain formation involves membrane proteins interacting with...
3.2K
Vesicular Tubular Clusters01:45

Vesicular Tubular Clusters

2.6K
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...
2.6K

You might also read

Related Articles

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

Sort by
Same author

A permeable protein nanocage enables facile cargo loading and cytosolic protein delivery.

bioRxiv : the preprint server for biology·2026
Same author

Directed evolution of multimeric proteins is enabled by dual-compensatory gene duplication.

bioRxiv : the preprint server for biology·2026
Same author

Encapsulins in Terpene Biosynthesis: Enzyme Nanoreactors in Bacterial Secondary Metabolism.

Biochemistry·2026
Same author

Engineering Spatial Control of Bacterial Organelles.

bioRxiv : the preprint server for biology·2025
Same author

Engineering encapsulin nanocages for drug delivery.

Materials advances·2025
Same author

HIV-1 binds dynein directly to hijack microtubule transport machinery.

Science advances·2025

Related Experiment Video

Updated: Sep 18, 2025

Assembly and Characterization of Polyelectrolyte Complex Micelles
08:44

Assembly and Characterization of Polyelectrolyte Complex Micelles

Published on: March 2, 2020

10.9K

A Two-Component Pseudo-Icosahedral Protein Nanocompartment with Variable Shell Composition and Irregular Tiling.

Cassandra A Dutcher1, Michael P Andreas1, Tobias W Giessen1

  • 1Department of Biological Chemistry, University of Michigan Medical School, Ann Arbor, MI, 48109, USA.

Advanced Science (Weinheim, Baden-Wurttemberg, Germany)
|June 25, 2025
PubMed
Summary
This summary is machine-generated.

This study characterizes a novel two-component encapsulin, revealing how its distinct protein shells co-assemble. This expands understanding of protein shell assembly and engineering possibilities.

Keywords:
capsidencapsulinicosahedralself‐assemblytwo‐component

More Related Videos

Ligand Nano-cluster Arrays in a Supported Lipid Bilayer
10:34

Ligand Nano-cluster Arrays in a Supported Lipid Bilayer

Published on: April 23, 2017

7.1K
Method to Visualize and Analyze Membrane Interacting Proteins by Transmission Electron Microscopy
10:49

Method to Visualize and Analyze Membrane Interacting Proteins by Transmission Electron Microscopy

Published on: March 5, 2017

13.4K

Related Experiment Videos

Last Updated: Sep 18, 2025

Assembly and Characterization of Polyelectrolyte Complex Micelles
08:44

Assembly and Characterization of Polyelectrolyte Complex Micelles

Published on: March 2, 2020

10.9K
Ligand Nano-cluster Arrays in a Supported Lipid Bilayer
10:34

Ligand Nano-cluster Arrays in a Supported Lipid Bilayer

Published on: April 23, 2017

7.1K
Method to Visualize and Analyze Membrane Interacting Proteins by Transmission Electron Microscopy
10:49

Method to Visualize and Analyze Membrane Interacting Proteins by Transmission Electron Microscopy

Published on: March 5, 2017

13.4K

Area of Science:

  • Biochemistry
  • Structural Biology
  • Microbiology

Background:

  • Protein shells, like viral capsids and cellular encapsulins, are vital for compartmentalization.
  • Most known encapsulins utilize a single protein component with the Hong Kong 97 (HK97)-fold.

Purpose of the Study:

  • To characterize a novel two-component encapsulin from Streptomyces lydicus.
  • To investigate the assembly mechanisms and structural properties of its constituent proteins.

Main Methods:

  • Cryo-electron microscopy (cryo-EM) for structure determination.
  • 3D classification and cross-linking studies to analyze shell composition and assembly.
  • Differential assembly assays for individual and co-assembling components.

Main Results:

  • The study identified and characterized two distinct shell proteins in a Family 2B encapsulin.
  • Demonstrated differential assembly behaviors of the two components and their ability to form mixed shells.
  • Revealed irregular tiling in mixed shells through structural analysis, expanding known HK97-fold assembly modes.

Conclusions:

  • This research presents the first characterization of a two-component encapsulin, broadening the scope of known HK97-fold protein assembly.
  • The findings provide a foundation for future functional studies and engineering of these novel protein compartments.