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

Directing Proteins to the Rough Endoplasmic Reticulum01:34

Directing Proteins to the Rough Endoplasmic Reticulum

The organelle-specific signaling sequences direct proteins synthesized in the cytosol to their final destination like ER, mitochondria, peroxisomes, etc. Some of the proteins directed to ER are then trafficked via vesicles to other organelles within the cell or the extracellular environment through the Golgi complex. For example, the rough ER synthesizes soluble proteins for transportation to the lysosomes or secretion out of the cell. It can also synthesize transmembrane proteins that can...
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...
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...
ER Retrieval Pathway01:45

ER Retrieval Pathway

In the secretory pathway, vesicles transport proteins from one cellular compartment to another in forward transport to deliver the protein to its correct location. Occasionally, misfolded proteins and incorrect proteins escape their original compartments, and a retrieval pathway is used to return the escaped proteins to their original compartment.
The ER uses many checkpoints to prevent the entry of incorrectly folded or a resident protein as cargo onto a transport vesicle. These mechanisms...
Post-translational Translocation of Proteins to the RER01:27

Post-translational Translocation of Proteins to the RER

A sizable fraction of proteins destined for ER are first synthesized in the cell cytosol and then transported across the ER membrane–a process called post-translational translocation. Similar to cotranslationally translocated proteins, these proteins also use the Sec translocon complex to enter the ER lumen.
Targeting proteins to the ER
Hsp40 and Hsp70 chaperone molecules bind the translated proteins in the cytosol to prevent their folding. The chaperone binding helps to keep the signal...
Role of ER in the Secretory Pathway01:17

Role of ER in the Secretory Pathway

Eukaryotic cells have a special pathway that enables communication between various intracellular membrane-bound compartments and also with the extracellular environment. This pathway is termed as the secretory pathway.
Components of the secretory pathway
About a third of proteins synthesized in the cell are sorted via the secretory route. They shuffle between different compartments in membrane-bound vesicles until they reach their final destination. The main intracellular compartments involved...

You might also read

Related Articles

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

Sort by
Same author

Genomic landscape of drug binding and pharmacogenetic variation across diverse populations using SNPdrug3D.

Nature communications·2026
Same author

Amino Acid Variants at the P94 Position in <i>Staphylococcus aureus</i> Class a Sortase Modulate Substrate Binding and Enzyme Activity.

Biochemistry·2026
Same author

Amino acid variants at the P94 position in <i>Staphylococcus aureus</i> class A sortase modulate substrate binding and enzyme activity.

bioRxiv : the preprint server for biology·2026
Same author

A Putative Interaction between the Transmembrane Domains of <i>Streptococcus pyogenes</i> Sortase A and Its Endogenous Substrate M Protein Revealed by Molecular Dynamics Simulations.

The journal of physical chemistry. B·2025
Same author

A modular Uba1-nanobody fusion enables selective ubiquitin transfer to tagged E2 enzymes.

The Journal of biological chemistry·2025
Same author

A multivalent nanobody-drug conjugate to prevent and treat influenza virus infections.

Proceedings of the National Academy of Sciences of the United States of America·2025
Same journal

Correction: Characterization of Mast2 kinase defines structural features, regulation, and substrates.

The Journal of biological chemistry·2026
Same journal

Isotope-Edited ESEEM: A New Method for Probing Copper Binding Sites in Neurodegenerative Proteins.

The Journal of biological chemistry·2026
Same journal

Introduction to the Thematic Review Series on Intracellular Protein Degradation. The ubiquitous biology of intracellular protein degradation: a tribute to Alfred L. ("Fred") Goldberg.

The Journal of biological chemistry·2026
Same journal

Correction: Aromatic residue-rich amino-terminal segments of temporin L self-assemble into collagen-mimetic peptides with cell-adhesion properties.

The Journal of biological chemistry·2026
Same journal

YhbO is a DJ-1 family glyoxalase and α-oxoaldehyde hydratase that confers resistance to reactive carbonyl stress (112).

The Journal of biological chemistry·2026
Same journal

ARMH3 acts as a central scaffold at the Golgi/TGN through interactions with Arl5, GBF1, and PI4KB.

The Journal of biological chemistry·2026
See all related articles

Related Experiment Video

Updated: Jun 24, 2026

Stable DNA Motifs, 1D and 2D Nanostructures Constructed from Small Circular DNA Molecules
09:32

Stable DNA Motifs, 1D and 2D Nanostructures Constructed from Small Circular DNA Molecules

Published on: April 12, 2019

A straight path to circular proteins.

John M Antos1, Maximilian Wei-Lin Popp, Robert Ernst

  • 1Whitehead Institute for Biomedical Research, Massachusetts Institute of Technology, Cambridge, Massachusetts 02142, USA.

The Journal of Biological Chemistry
|April 11, 2009
PubMed
Summary
This summary is machine-generated.

Researchers developed a novel, efficient method for creating stable circular proteins using sortase-catalyzed cyclization. This technique offers improved protein stability and refolding properties for laboratory and in vivo applications.

More Related Videos

Use of Alu Element Containing Minigenes to Analyze Circular RNAs
13:10

Use of Alu Element Containing Minigenes to Analyze Circular RNAs

Published on: March 10, 2020

Large-scale Production of Recombinant RNAs on a Circular Scaffold Using a Viroid-derived System in Escherichia coli
10:38

Large-scale Production of Recombinant RNAs on a Circular Scaffold Using a Viroid-derived System in Escherichia coli

Published on: November 30, 2018

Related Experiment Videos

Last Updated: Jun 24, 2026

Stable DNA Motifs, 1D and 2D Nanostructures Constructed from Small Circular DNA Molecules
09:32

Stable DNA Motifs, 1D and 2D Nanostructures Constructed from Small Circular DNA Molecules

Published on: April 12, 2019

Use of Alu Element Containing Minigenes to Analyze Circular RNAs
13:10

Use of Alu Element Containing Minigenes to Analyze Circular RNAs

Published on: March 10, 2020

Large-scale Production of Recombinant RNAs on a Circular Scaffold Using a Viroid-derived System in Escherichia coli
10:38

Large-scale Production of Recombinant RNAs on a Circular Scaffold Using a Viroid-derived System in Escherichia coli

Published on: November 30, 2018

Area of Science:

  • Biochemistry and Molecular Biology
  • Protein Engineering

Background:

  • Protein folding and stability are critical for protein function and behavior.
  • Cyclic peptides and proteins often exhibit enhanced stability against denaturation and proteolysis compared to linear forms.
  • Existing methods for producing circular proteins, such as native chemical ligation and intein-based approaches, have limitations for larger proteins.

Purpose of the Study:

  • To develop a novel, efficient, and reversible method for creating circular proteins.
  • To investigate the application of sortase-catalyzed reactions for protein cyclization.
  • To assess the impact of circularization on protein stability and refolding properties.

Main Methods:

  • Utilized a sortase-catalyzed cyclization reaction.
  • Required minimal modification of the target protein for cyclization.
  • Demonstrated reversible circular protein formation.

Main Results:

  • Achieved excellent efficiency in sortase-catalyzed protein cyclization.
  • The developed method allows for reversible formation of circular proteins.
  • Circularization via this method is applicable with minimal protein modification.

Conclusions:

  • Sortase-catalyzed cyclization provides an efficient and reversible strategy for producing circular proteins.
  • This method enhances protein stability and refolding properties.
  • The technique has significant implications for protein engineering, structural analysis, and in vivo applications.