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

GPI Anchoring of Proteins in the ER Membrane01:29

GPI Anchoring of Proteins in the ER Membrane

5.5K
GPI-anchoring is a post-translational, reversible protein modification that is ubiquitous in eukaryotes. Such proteins are primarily present on the exoplasmic leaflet of the plasma membrane.
GPI-anchor structure
A sequence of 11 enzymatic reactions results in the synthesis of the complete GPI anchor consisting of a hydrophobic and a hydrophilic portion. The hydrophobic portion comprises phosphatidylinositol, while the hydrophilic part comprises polar groups like phosphoethanolamine,...
5.5K
Tail-anchoring of Proteins in the ER Membrane01:45

Tail-anchoring of Proteins in the ER Membrane

3.8K
Tail-anchored, or TA, proteins are estimated to make up to 3-5% of membrane proteins found in the eukaryotic cell. Such proteins have a single transmembrane domain located approximately 30 amino acid residues upstream from the C-terminal end. As a result, the signal recognition particle (SRP) cannot guide a TA protein to the ER membrane for cotranslational insertion. Hence, they are integrated into the ER membrane post-translationally using their C-terminal end as the anchor. TA proteins...
3.8K
The Anchoring-and-Adjustment Heuristic01:25

The Anchoring-and-Adjustment Heuristic

7.8K
In order to make good decisions, we use our knowledge and our reasoning. Often, this knowledge and reasoning is sound and solid. However, sometimes, we are swayed by biases or by others manipulating a situation. For example, let’s say you and three friends wanted to rent a house and had a combined target budget of $1,600. The realtor shows you only very run-down houses for $1,600 and then shows you a very nice house for $2,000. Might you ask each person to pay more in rent to get the...
7.8K
Anchoring Junctions01:03

Anchoring Junctions

5.0K
Anchoring junctions are multiprotein complexes that help cells connect to other cells and the extracellular matrix. Anchoring junctions are present on the lateral and basal surfaces of cells, providing strong and flexible connections. Focal adhesions are often formed due to cell interactions with the ECM substrata, which initiate signal transduction via kinase cascades and other mechanisms. Together, they provide stability and tissue integrity. There are three types of anchoring junctions:...
5.0K
Lipids as Anchors01:32

Lipids as Anchors

7.4K
In the plasma membrane, the lipids forming the bilayer can also act as an anchor to tether proteins to the membrane. The three main types of lipid anchors found in eukaryotes are – prenyl groups, fatty acyl groups, and glycosylphosphatidylinositol or GPI groups. Prenyl and fatty acyl groups act as anchors on the cytosolic surface of the membrane, whereas GPI anchors proteins on the extracellular side.
The carboxy-terminal of most of the prenylated proteins, such as Ras proteins, contains...
7.4K
Introduction to Membrane Proteins01:16

Introduction to Membrane Proteins

81.1K
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...
81.1K

You might also read

Related Articles

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

Sort by
Same author

FtsZ forms biomolecular condensates in a polar-growing Alphaproteobacterium.

mBio·2026
Same author

Mechanistic Insights into the Antimicrobial Effect of Benzodioxane-Benzamides Against <i>Escherichia coli</i>.

Antibiotics (Basel, Switzerland)·2026
Same author

Benzodioxane-benzamides targeting bacterial cell division protein FtsZ potentially disrupt SlmA-mediated nucleoid occlusion and reversible biomolecular condensation.

International journal of biological macromolecules·2025
Same author

Conjugative delivery of toxin genes <i>ccdB</i> and <i>kil</i> confers synergistic killing of bacterial recipients.

Journal of bacteriology·2025
Same author

Ribosome deficiency induces <i>Salmonella</i> filamentation within host cells.

mBio·2025
Same author

Evidence for biomolecular condensates formed by the Escherichia coli MatP protein in spatiotemporal regulation of the bacterial cell division cycle.

International journal of biological macromolecules·2025

Related Experiment Video

Updated: Feb 2, 2026

Detection of Detergent-sensitive Interactions Between Membrane Proteins
10:09

Detection of Detergent-sensitive Interactions Between Membrane Proteins

Published on: March 7, 2018

6.3K

Direct Interaction between the Two Z Ring Membrane Anchors FtsA and ZipA.

Daniel E Vega1, William Margolin2

  • 1Department of Microbiology and Molecular Genetics, McGovern Medical School, University of Texas, Houston, Texas, USA.

Journal of Bacteriology
|November 28, 2018
PubMed
Summary

The bacterial cell division proteins FtsA and ZipA directly interact at midcell. This interaction, involving FtsA helix 7, suggests FtsA and ZipA regulate each other

Keywords:
Escherichia colicell divisioncross-linkingftsAftsZzipA

More Related Videos

Evaluation of Protein&#8211;Protein Interactions using an On-Membrane Digestion Technique
07:07

Evaluation of Protein–Protein Interactions using an On-Membrane Digestion Technique

Published on: July 19, 2019

7.1K
Membrane-SPINE: A Biochemical Tool to Identify Protein-protein Interactions of Membrane Proteins In Vivo
10:53

Membrane-SPINE: A Biochemical Tool to Identify Protein-protein Interactions of Membrane Proteins In Vivo

Published on: November 7, 2013

14.1K

Related Experiment Videos

Last Updated: Feb 2, 2026

Detection of Detergent-sensitive Interactions Between Membrane Proteins
10:09

Detection of Detergent-sensitive Interactions Between Membrane Proteins

Published on: March 7, 2018

6.3K
Evaluation of Protein&#8211;Protein Interactions using an On-Membrane Digestion Technique
07:07

Evaluation of Protein–Protein Interactions using an On-Membrane Digestion Technique

Published on: July 19, 2019

7.1K
Membrane-SPINE: A Biochemical Tool to Identify Protein-protein Interactions of Membrane Proteins In Vivo
10:53

Membrane-SPINE: A Biochemical Tool to Identify Protein-protein Interactions of Membrane Proteins In Vivo

Published on: November 7, 2013

14.1K

Area of Science:

  • Microbiology
  • Cell Biology
  • Biochemistry

Background:

  • Bacterial cell division is orchestrated by a protein machine at midcell, involving FtsZ, FtsA, and ZipA.
  • FtsZ forms a ring, tethered to the membrane by FtsA and ZipA, crucial for division.
  • The precise roles of FtsA and ZipA as separate membrane tethers for FtsZ remain unclear.

Purpose of the Study:

  • To investigate the potential direct interaction between FtsA and ZipA.
  • To identify the molecular interface mediating the FtsA-ZipA interaction.
  • To understand how this interaction contributes to the regulation of bacterial cell division.

Main Methods:

  • In vivo cross-linking experiments were employed to detect protein-protein interactions.
  • Mutagenesis and biochemical assays were used to map the interaction interface.
  • Analysis focused on the role of FtsA helix 7 in binding ZipA.

Main Results:

  • Direct interaction between FtsA and ZipA was confirmed using in vivo cross-linking.
  • FtsA helix 7 was identified as a key interface for ZipA binding.
  • This helix is also involved in FtsA's ATP binding, suggesting a regulatory role.

Conclusions:

  • FtsA and ZipA directly interact, challenging previous assumptions.
  • The FtsA-ZipA interaction, mediated by FtsA helix 7, implies a regulatory crosstalk between these essential division proteins.
  • This finding provides new insights into the complex mechanism of bacterial cell division regulation.