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

Protein Complex Assembly02:41

Protein Complex Assembly

17.1K
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...
17.1K
Protein Complex Assembly02:41

Protein Complex Assembly

2.7K
2.7K
Porin Insertion in the Outer Mitochondrial Membrane01:12

Porin Insertion in the Outer Mitochondrial Membrane

5.2K
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...
5.2K
Assembly of Cytoskeletal Filaments01:18

Assembly of Cytoskeletal Filaments

28.4K
Cytoskeletal filaments are polymeric forms of smaller protein subunits. However, individual cytoskeletal filaments may easily disassemble or associate with other similar filaments to form rigid structures. Microfilaments, made of actin monomers, rely on actin-binding proteins to form bundles and create networks of individual actin filaments. Microtubules rely on microtubule-associated proteins (MAPs) to form sturdy cylindrical structures. However, the proteins involved in forming complex...
28.4K
Assembly of Signaling Complexes01:30

Assembly of Signaling Complexes

7.2K
Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
7.2K
Coat Assembly and GTPases01:33

Coat Assembly and GTPases

4.7K
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...
4.7K

You might also read

Related Articles

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

Sort by
Same author

De novo design of miniproteins targeting GPCRs.

Nature·2026
Same author

Mechanism of phospholipid transport to the bacterial outer membrane by TAM.

bioRxiv : the preprint server for biology·2026
Same author

<i>Staphylococcus</i> species infected by a bacteriophage with a tail that is both curved and contractile.

mBio·2026
Same author

In vivo functional profiling and structural characterization of the human <i>GLP1R</i> A316T variant.

Science advances·2026
Same author

Chemical inhibition of MrkH-dependent activation of type 3 fimbriae synthesis and biofilm formation by Klebsiella pneumoniae.

NPJ biofilms and microbiomes·2025
Same author

Unconventional binding of calmodulin to CHK2 kinase inhibits catalytic activity.

The Biochemical journal·2025

Related Experiment Video

Updated: Apr 1, 2026

The MultiBac Protein Complex Production Platform at the EMBL
13:51

The MultiBac Protein Complex Production Platform at the EMBL

Published on: July 11, 2013

16.7K

The β-Barrel Assembly Machinery Complex.

Denisse L Leyton1, Matthew J Belousoff2, Trevor Lithgow3

  • 1Research School of Biology, Australian National University, Canberra, ACT, 0200, Australia. denisse.leyton@anu.edu.au.

Methods in Molecular Biology (Clifton, N.J.)
|October 3, 2015
PubMed
Summary
This summary is machine-generated.

The bacterial beta-barrel assembly machinery (BAM) complex, particularly BamA, is crucial for integrating outer membrane proteins in gram-negative bacteria. This work reviews the mechanisms and methods used to study BAM complex function in protein biogenesis.

Keywords:
BamAOmp85Outer membraneOuter membrane β-barrel proteins (OMPs)Periplasmic chaperonesβ-barrelβ-barrel assembly machinery (BAM)

More Related Videos

Simulation of a Scaled Assembly Process with Collaboration of a Robotic Arm and Monitoring through a Vision System for Quality Control
05:47

Simulation of a Scaled Assembly Process with Collaboration of a Robotic Arm and Monitoring through a Vision System for Quality Control

Published on: August 29, 2025

620
Examining Proteasome Assembly with Recombinant Archaeal Proteasomes and Nondenaturing PAGE: The Case for a Combined Approach
09:57

Examining Proteasome Assembly with Recombinant Archaeal Proteasomes and Nondenaturing PAGE: The Case for a Combined Approach

Published on: December 17, 2016

7.0K

Related Experiment Videos

Last Updated: Apr 1, 2026

The MultiBac Protein Complex Production Platform at the EMBL
13:51

The MultiBac Protein Complex Production Platform at the EMBL

Published on: July 11, 2013

16.7K
Simulation of a Scaled Assembly Process with Collaboration of a Robotic Arm and Monitoring through a Vision System for Quality Control
05:47

Simulation of a Scaled Assembly Process with Collaboration of a Robotic Arm and Monitoring through a Vision System for Quality Control

Published on: August 29, 2025

620
Examining Proteasome Assembly with Recombinant Archaeal Proteasomes and Nondenaturing PAGE: The Case for a Combined Approach
09:57

Examining Proteasome Assembly with Recombinant Archaeal Proteasomes and Nondenaturing PAGE: The Case for a Combined Approach

Published on: December 17, 2016

7.0K

Area of Science:

  • Microbiology
  • Structural Biology
  • Biochemistry

Background:

  • Gram-negative bacteria possess essential outer membrane proteins with beta-barrel structures.
  • The beta-barrel assembly machinery (BAM) complex facilitates the integration of these proteins into the outer membrane.
  • BamA is a conserved, central component of the BAM complex, also present in eukaryotic organelles.

Purpose of the Study:

  • To provide an overview of the mechanisms by which the BAM complex drives beta-barrel assembly.
  • To introduce the methodologies and challenges in studying BAM complex function.

Main Methods:

  • Review of existing literature on BAM complex structure and function.
  • Discussion of experimental protocols and techniques used in relevant studies.

Main Results:

  • The BAM complex, with BamA as the core subunit, is essential for outer membrane protein biogenesis.
  • BamA interacts with lipoproteins (BamB, C, D, E) to facilitate its function.
  • Studies have elucidated the mechanism of BAM-mediated beta-barrel protein integration.

Conclusions:

  • Understanding the BAM complex is key to comprehending essential processes in gram-negative bacteria.
  • The reviewed methodologies offer insights into overcoming challenges in studying membrane protein biogenesis.