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

Porin Insertion in the Outer Mitochondrial Membrane01:12

Porin Insertion in the Outer Mitochondrial Membrane

5.4K
Porins are beta-barrel proteins translocated to the mitochondrial outer membrane through the TOM complex into the intermembrane space. Porin precursors bind TIM chaperones within the intermembrane space and are guided to the Sorting and Assembly Machinery complex or SAM complex on the outer mitochondrial membrane.
Three models describe the assembly of porins by the SAM complex and their insertion into the outer membrane. Model 1 suggests that porins are assembled outside the SAM channel as the...
5.4K
Multi-pass Transmembrane Proteins and β-barrels01:09

Multi-pass Transmembrane Proteins and β-barrels

6.9K
In multi-pass transmembrane proteins, the polypeptide chain crosses the membrane more than once. The transmembrane polypeptide chain either forms an α-helix or β-strand structure. α-Helix containing multi-pass transmembrane proteins are ubiquitous, whereas β-strand containing ones are mainly found in gram-negative bacteria, mitochondria, and chloroplasts.
α-Helix containing multi-pass transmembrane proteins
Multi-pass transmembrane proteins such as...
6.9K
Structure of Porins01:21

Structure of Porins

4.2K
Mitochondria, chloroplasts, and gram-negative bacteria have transmembrane, beta-barrel proteins called porins to mediate the free diffusion of ions and metabolites across the membrane. Mitochondrial porin precursors contain conserved amino acid sequences called beta signals at their C-terminal. Beta signals have a  motif of PoXGXXHyXHy (Po-Polar, X-Any amino acid, G-Glycine, Hy-LargeHydrophobic), which are crucial for precursor recognition to initiate precursor assembly. Beta-barrel...
4.2K
Protein Complex Assembly02:41

Protein Complex Assembly

2.7K
2.7K
Protein Complex Assembly02:41

Protein Complex Assembly

17.3K
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...
17.3K
Coat Assembly and GTPases01:33

Coat Assembly and GTPases

4.8K
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...
4.8K

You might also read

Related Articles

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

Sort by
Same author

Second-line systemic treatment for metastatic colorectal cancer: A systematic review and Bayesian network meta-analysis based on RCT.

PloS one·2024
Same author

Performance of radiomics in preoperative determination of malignant potential and Ki-67 expression levels in gastrointestinal stromal tumors: a systematic review and meta-analysis.

Acta radiologica (Stockholm, Sweden : 1987)·2024
Same author

Signal peptide replacement of Ag43 enables an efficient bacterial cell surface display of receptor-binding domain of coronavirus.

Biochemical and biophysical research communications·2024
Same author

A minimum functional form of the Escherichia coli BAM complex constituted by BamADE assembles outer membrane proteins in vitro.

The Journal of biological chemistry·2024
Same author

Licochalcone A inhibits the assembly function of β-barrel assembly machinery in Escherichia coli.

Biochemical and biophysical research communications·2023
Same author

What Approaches to Thwart Bacterial Efflux Pumps-Mediated Resistance?

Antibiotics (Basel, Switzerland)·2022

Related Experiment Video

Updated: Apr 19, 2026

Visualizing Protein Kinase A Activity In Head-fixed Behaving Mice Using In Vivo Two-photon Fluorescence Lifetime Imaging Microscopy
10:41

Visualizing Protein Kinase A Activity In Head-fixed Behaving Mice Using In Vivo Two-photon Fluorescence Lifetime Imaging Microscopy

Published on: June 7, 2019

9.2K

TtOmp85, a β-barrel assembly protein, functions by barrel augmentation.

Luisa Estrada Mallarino1, Enguo Fan, Meike Odermatt

  • 1Department of Biology, University of Konstanz , Universitätsstraße 10, 78457 Konstanz, Germany.

Biochemistry
|December 25, 2014
PubMed
Summary

Outer membrane proteins are inserted by Omp85/BamA family proteins. TtoA protein insertion into liposomes by an Omp85 homologue suggests a compound channel model for protein transport.

More Related Videos

X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050
11:27

X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050

Published on: May 13, 2020

4.5K
Updated Protocol for the Assembly and Use of the Minibioreactor Array (MBRA)
09:38

Updated Protocol for the Assembly and Use of the Minibioreactor Array (MBRA)

Published on: September 5, 2025

1.1K

Related Experiment Videos

Last Updated: Apr 19, 2026

Visualizing Protein Kinase A Activity In Head-fixed Behaving Mice Using In Vivo Two-photon Fluorescence Lifetime Imaging Microscopy
10:41

Visualizing Protein Kinase A Activity In Head-fixed Behaving Mice Using In Vivo Two-photon Fluorescence Lifetime Imaging Microscopy

Published on: June 7, 2019

9.2K
X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050
11:27

X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050

Published on: May 13, 2020

4.5K
Updated Protocol for the Assembly and Use of the Minibioreactor Array (MBRA)
09:38

Updated Protocol for the Assembly and Use of the Minibioreactor Array (MBRA)

Published on: September 5, 2025

1.1K

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • Outer membrane proteins are essential for Gram-negative bacteria and their derived organelles.
  • The Omp85/BamA protein family facilitates the insertion of proteins into the outer membrane.

Purpose of the Study:

  • To investigate the insertion and folding mechanism of the outer membrane protein TtoA.
  • To elucidate the role of Omp85 homologues in protein transport across membranes.

Main Methods:

  • Studied the insertion and folding of TtoA into liposomes mediated by an Omp85 homologue.
  • Measured channel conductance of Omp85 in black lipid membranes with and without TtoA peptides.

Main Results:

  • An eight-stranded outer membrane protein, TtoA, was successfully inserted and folded into liposomes by an Omp85 homologue.
  • Compound channels formed by Omp85 and TtoA peptides exhibited higher conductance than Omp85 alone.
  • Data support a model of sequential augmentation of the Omp85 beta-barrel by incoming outer membrane proteins.

Conclusions:

  • Omp85 homologues facilitate the insertion of outer membrane proteins like TtoA.
  • A compound channel model involving sequential beta-strand augmentation is proposed for outer membrane protein biogenesis.