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

4.8K
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...
4.8K
Multi-pass Transmembrane Proteins and β-barrels01:09

Multi-pass Transmembrane Proteins and β-barrels

6.5K
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...
6.5K
Protein Transport to the Outer Chloroplast Membrane01:11

Protein Transport to the Outer Chloroplast Membrane

2.4K
Chloroplast outer membrane proteins encoded by the nucleus are synthesized in the cytosol. Soon after synthesis, they bind cytosolic factors such as 14-3-3 protein and the Hsp70 chaperones that keep these precursors in an unfolded state until their translocation.
Two models describe the mechanism of precursor recognition and entry across the outer membrane through the TOC complex. Model 1 suggests the newly synthesized precursor binds to the TOC receptor 159 and forms a complex.
2.4K
Protein Complex Assembly02:41

Protein Complex Assembly

16.7K
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...
16.7K
Protein Complex Assembly02:41

Protein Complex Assembly

2.6K
2.6K
Introduction to Membrane Proteins01:16

Introduction to Membrane Proteins

80.9K
The cell membrane, or plasma membrane, is an ever-changing landscape. It is described as a fluid mosaic where various macromolecules are embedded in the phospholipid bilayer. Among the macromolecules are proteins. The protein content varies across cell types. For example, mitochondrial inner membranes contain ~76% protein content, while myelin contains ~18% protein content. Individual cells contain many types of membrane proteins—red blood cells contain over 50—and different cell...
80.9K

You might also read

Related Articles

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

Sort by
Same author

A mechanism for substrate quality control in outer membrane protein assembly.

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

Synthetic overlapping genes stabilize genetic systems.

mBio·2026
Same author

Synthetic communities as a model for determining interactions between a biofertilizer chassis organism and native microbial consortia.

The ISME journal·2025
Same author

OmpA controls order in the outer membrane and shares the mechanical load.

Proceedings of the National Academy of Sciences of the United States of America·2024
Same author

Periplasmic Chaperones: Outer Membrane Biogenesis and Envelope Stress.

Annual review of microbiology·2024
Same author

Global protein turnover quantification in Escherichia coli reveals cytoplasmic recycling under nitrogen limitation.

Nature communications·2024
Same journal

A history of <i>EcoSal Plus</i>.

EcoSal Plus·2025
Same journal

Transcriptional reprogramming by bacteriophage T4: turning the host transcriptional machinery to the dark side.

EcoSal Plus·2025
Same journal

Bacteriophage T4 genome packaging: mechanism and application.

EcoSal Plus·2025
Same journal

The bacteriophage T4 homologous recombination system: mechanism, applications, conservation, and environmental significance.

EcoSal Plus·2025
Same journal

The bacteriophage T4 replisome: a model system for understanding DNA replication mechanisms.

EcoSal Plus·2025
Same journal

Biology of host-dependent restriction-modification in prokaryotes.

EcoSal Plus·2025
See all related articles

Related Experiment Video

Updated: Jan 27, 2026

From Constructs to Crystals &#8211; Towards Structure Determination of &#946;-barrel Outer Membrane Proteins
09:55

From Constructs to Crystals – Towards Structure Determination of β-barrel Outer Membrane Proteins

Published on: July 4, 2016

14.0K

Outer Membrane Protein Insertion by the β-barrel Assembly Machine.

Dante P Ricci1, Thomas J Silhavy2

  • 1Department of Early Research, Achaogen, Inc., South San Francisco, CA 94080.

Ecosal Plus
|March 15, 2019
PubMed
Summary
This summary is machine-generated.

Gram-negative bacteria use the β-barrel assembly machine (Bam) to integrate outer membrane proteins. This review explores recent insights into the mechanism of Bam-assisted outer membrane protein assembly.

More Related Videos

Co-Translational Insertion of Membrane Proteins into Preformed Nanodiscs
08:24

Co-Translational Insertion of Membrane Proteins into Preformed Nanodiscs

Published on: November 19, 2020

3.9K
Crystallizing Membrane Proteins for Structure Determination using Lipidic Mesophases
22:00

Crystallizing Membrane Proteins for Structure Determination using Lipidic Mesophases

Published on: November 21, 2010

30.6K

Related Experiment Videos

Last Updated: Jan 27, 2026

From Constructs to Crystals &#8211; Towards Structure Determination of &#946;-barrel Outer Membrane Proteins
09:55

From Constructs to Crystals – Towards Structure Determination of β-barrel Outer Membrane Proteins

Published on: July 4, 2016

14.0K
Co-Translational Insertion of Membrane Proteins into Preformed Nanodiscs
08:24

Co-Translational Insertion of Membrane Proteins into Preformed Nanodiscs

Published on: November 19, 2020

3.9K
Crystallizing Membrane Proteins for Structure Determination using Lipidic Mesophases
22:00

Crystallizing Membrane Proteins for Structure Determination using Lipidic Mesophases

Published on: November 21, 2010

30.6K

Area of Science:

  • Microbiology
  • Structural Biology
  • Biochemistry

Background:

  • Gram-negative bacteria possess a unique outer membrane (OM) essential for their survival.
  • Integral OM proteins, primarily β-barrel proteins, are synthesized in the cytoplasm and must be transported and assembled into the OM.
  • The β-barrel assembly machine (Bam) complex is conserved across Gram-negative bacteria and is responsible for OM protein integration.

Purpose of the Study:

  • To review mechanistic analyses of OM β-barrel protein folding.
  • To summarize recent insights into the dynamics of the Bam complex.
  • To propose a general model for OM protein recognition and assembly by Bam.

Main Methods:

  • Review of existing literature on OM protein folding.
  • Analysis of studies on Bam complex dynamics.
  • Synthesis of recent findings to inform a mechanistic model.

Main Results:

  • While Bam components are well-characterized, the precise mechanism of OM protein integration remains unclear.
  • Recent studies provide new perspectives on protein folding pathways and Bam complex interactions.
  • These insights are crucial for understanding how β-barrel proteins are recognized and assembled.

Conclusions:

  • A comprehensive model for Bam-assisted OM protein assembly is emerging.
  • Understanding this process is vital for deciphering Gram-negative bacterial envelope biogenesis.
  • Further research into Bam dynamics and protein interactions will refine this model.