Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

ATP Synthase: Structure

ATP Synthase: Structure

ATP synthase or ATPase is among the most conserved proteins found in bacteria, mammals, and plants. This enzyme can catalyze a forward reaction in response to the electrochemical gradient, producing ATP from ADP and inorganic phosphate. ATP synthase can also work in a reverse direction by hydrolyzing ATP and generating an electrochemical gradient. Different forms of ATP synthases have evolved special features to meet the specific demands of the cell. Based on their specific feature, ATP...

ATP Synthase: Mechanism

ATP Synthase: Mechanism

In animals, the mitochondrial F1F0 ATP synthase is the key protein that synthesizes ATP molecules through a complex catalytic mechanism. While the nuclear genome encodes the majority of ATP synthase subunits, the mitochondrial genome encodes some of the enzyme's most critical components. The formation of this multi-subunit enzyme is a complex multi-step process regulated at the level of transcription, translation, and assembly. Defects in one or more of these steps can result in decreased...

Protein Complex Assembly

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...

Protein Complex Assembly

Protein Complex Assembly

Spindle Assembly

Spindle Assembly

Spindle assembly occurs through three, often coexisting, pathways – the centrosome-mediated pathway, the chromatin-mediated pathway, and the microtubule-mediated pathway – collectively contributing to form a robust spindle apparatus.
In most cells, centrosomes are the primary microtubule nucleation centers. In the centrosome-mediated pathway, the G2-prophase transition triggers centrosome maturation and increased microtubule nucleation. Progressive nucleation results in a...

Oligosaccharide Assembly

Oligosaccharide Assembly

Protein glycosylation starts in the ER lumen and continues in the Golgi apparatus. Glycosyltransferases catalyze the addition of sugar molecules or glycosylation of proteins. Usually, these enzymes add sugars to the hydroxyl groups of selected serine or threonine residues to form O-linked glycans or the amino groups of asparagine residues to form N-linked glycans. Different positions on the same polypeptide chain can contain differently linked glycans.
Multiple sugar molecules that may or may...

You might also read

Related Articles

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

Sort by

Same author

From First Principles to Function: How AI Is Reshaping Enzyme Design.

Biochemistry·2026

Same author

An engineered closed-shell, two-component, 480-subunit nucleocapsid.

Proceedings of the National Academy of Sciences of the United States of America·2026

Same author

A molecular basis for stoichiometric enzyme encapsulation in the vitamin B2 biosynthesis compartment.

Nature communications·2026

Same author

Identification of overoxidizing and non-overoxidizing NAD-dependent methanol dehydrogenases and implications for synthetic methylotrophy.

Nature communications·2025

Same author

Computational design of cysteine proteases.

bioRxiv : the preprint server for biology·2025

Same author

Computational design of metalloproteases.

bioRxiv : the preprint server for biology·2025

Search research articles

Related Experiment Video

Updated: Feb 11, 2026

A Colorimetric Assay of Citrate Synthase Activity in Drosophila Melanogaster

A Colorimetric Assay of Citrate Synthase Activity in Drosophila Melanogaster

Published on: January 16, 2020

Tailoring lumazine synthase assemblies for bionanotechnology.

Yusuke Azuma¹, Thomas G W Edwardson, Donald Hilvert

¹Laboratory of Organic Chemistry, ETH Zurich, 8093 Zurich, Switzerland. hilvert@org.chem.ethz.ch.

Chemical Society Reviews

|May 2, 2018

Summary

Engineered protein cages, derived from lumazine synthase, serve as versatile nanoscale platforms. These adaptable scaffolds are modified for applications in nanoreactors, artificial organelles, and drug delivery systems.

More Related Videos

Construction of Synthetic Phage Displayed Fab Library with Tailored Diversity

Construction of Synthetic Phage Displayed Fab Library with Tailored Diversity

Published on: May 1, 2018

Modification and Functionalization of the Guanidine Group by Tailor-made Precursors

Modification and Functionalization of the Guanidine Group by Tailor-made Precursors

Published on: April 27, 2017

Related Experiment Videos

Last Updated: Feb 11, 2026

A Colorimetric Assay of Citrate Synthase Activity in Drosophila Melanogaster

A Colorimetric Assay of Citrate Synthase Activity in Drosophila Melanogaster

Published on: January 16, 2020

Construction of Synthetic Phage Displayed Fab Library with Tailored Diversity

Construction of Synthetic Phage Displayed Fab Library with Tailored Diversity

Published on: May 1, 2018

Modification and Functionalization of the Guanidine Group by Tailor-made Precursors

Modification and Functionalization of the Guanidine Group by Tailor-made Precursors

Published on: April 27, 2017

Area of Science:

Biotechnology
Nanotechnology
Protein Engineering

Background:

Hierarchical protein self-assembly creates nanoscale compartments valuable for nanotechnology.
Protein cages offer well-defined structures and chemical functionality, enabling diverse applications through genetic and chemical modification.

Purpose of the Study:

To review the engineering progress of lumazine synthase, a cage-forming enzyme.
To highlight the versatility of this bacterial nanocompartment as a malleable scaffold.

Main Methods:

Summarizing advancements in the genetic and chemical modification of lumazine synthase.
Reviewing the diversification of the natural protein into unique proteinaceous capsules.

Main Results:

Lumazine synthase has been engineered into a family of versatile protein cages.
These engineered cages have been modified and assembled with other components.

Conclusions:

Engineered lumazine synthase provides a robust platform for creating functional nanomaterials.
Applications include nanoreactors, artificial organelles, delivery vehicles, and virus mimics.