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

Porin Insertion in the Outer Mitochondrial Membrane

Porin Insertion in the Outer Mitochondrial Membrane

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...

You might also read

Related Articles

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

Sort by

Same author

Dipeptidyl peptidase 3 sets the threshold for immune activation and survival during experimental bacterial infection.

Nature communications·2026

Same author

The Proteomics-Based Stratification of Obese Subjects Allows for a Second Selective Level Beyond Gender Classification.

International journal of molecular sciences·2026

Same author

Conserved and acquired: Decoding YbjX and VirK in the pathogenicity of <i>Shigella flexneri</i>.

Virulence·2025

Same author

Effects of Dietary Sodium Modulation on Circulating Extracellular Vesicles.

Hypertension (Dallas, Tex. : 1979)·2025

Same author

Synovial MS4A4A correlates with inflammation and counteracts response to corticosteroids in arthritis.

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

Same author

A novel peptidoglycan deacetylase modulates daughter cell separation in E. coli.

PLoS genetics·2025

Search research articles

Related Experiment Video

Updated: Apr 27, 2026

Identification of Antibacterial Immunity Proteins in Escherichia coli using MALDI-TOF-TOF-MS/MS and Top-Down Proteomic Analysis

Identification of Antibacterial Immunity Proteins in Escherichia coli using MALDI-TOF-TOF-MS/MS and Top-Down Proteomic Analysis

Published on: May 23, 2021

Dissecting Escherichia coli outer membrane biogenesis using differential proteomics.

Alessandra M Martorana¹, Sara Motta², Dario Di Silvestre²

¹Dipartimento di Biotecnologie e Bioscienze, Università di Milano-Bicocca, Milan, Italy.

|June 27, 2014

Summary

This summary is machine-generated.

Gram-negative bacteria use the LptA-G protein complex to transport lipopolysaccharide (LPS) to the outer membrane. Disrupting this transport triggers cellular responses involving cell envelope biogenesis, division, and protein folding.

More Related Videos

Identification of Protein Complexes in Escherichia coli using Sequential Peptide Affinity Purification in Combination with Tandem Mass Spectrometry

Identification of Protein Complexes in Escherichia coli using Sequential Peptide Affinity Purification in Combination with Tandem Mass Spectrometry

Published on: November 12, 2012

Directed Protein Packaging within Outer Membrane Vesicles from Escherichia coli: Design, Production and Purification

Directed Protein Packaging within Outer Membrane Vesicles from Escherichia coli: Design, Production and Purification

Published on: November 16, 2016

Related Experiment Videos

Last Updated: Apr 27, 2026

Identification of Antibacterial Immunity Proteins in Escherichia coli using MALDI-TOF-TOF-MS/MS and Top-Down Proteomic Analysis

Identification of Antibacterial Immunity Proteins in Escherichia coli using MALDI-TOF-TOF-MS/MS and Top-Down Proteomic Analysis

Published on: May 23, 2021

Identification of Protein Complexes in Escherichia coli using Sequential Peptide Affinity Purification in Combination with Tandem Mass Spectrometry

Identification of Protein Complexes in Escherichia coli using Sequential Peptide Affinity Purification in Combination with Tandem Mass Spectrometry

Published on: November 12, 2012

Directed Protein Packaging within Outer Membrane Vesicles from Escherichia coli: Design, Production and Purification

Directed Protein Packaging within Outer Membrane Vesicles from Escherichia coli: Design, Production and Purification

Published on: November 16, 2016

Area of Science:

Microbiology
Molecular Biology
Bacterial Cell Envelope Biogenesis

Background:

Gram-negative bacteria possess a complex cell envelope with an outer membrane essential for viability.
Lipopolysaccharide (LPS) is a critical glycolipid in the outer membrane, determining its unique properties.
The LptA-G protein complex facilitates LPS transport across the cell envelope.

Purpose of the Study:

To investigate the global cellular response of Escherichia coli to defects in LPS transport.
To identify proteins modulated during impaired LPS transport to the outer membrane.

Main Methods:

Differential proteomics using Multidimensional Protein Identification Technology (MudPIT).
Analysis of the envelope proteome in an lptC conditional mutant under permissive and non-permissive conditions.

Main Results:

Identified 123 proteins with altered levels upon LptC depletion, indicating a significant cellular response.
Modulated proteins are primarily involved in cell envelope biogenesis, peptidoglycan remodeling, cell division, and protein folding.
LPS transport defects trigger a coordinated response to maintain outer membrane functionality.

Conclusions:

E. coli mounts a comprehensive response to disruptions in LPS transport.
Understanding these responses is crucial for comprehending cell envelope homeostasis and bacterial viability.
This study provides insights into the adaptive mechanisms of bacteria facing envelope stress.