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

Mechanisms of Membrane Domain Formation00:59

Mechanisms of Membrane Domain Formation

3.8K
Different physical properties of lipids and proteins allow them to localize and form distinct islands or domains in the membrane. Some membrane domains are formed due to protein-protein interactions, whereas others are formed due to the presence of specific lipids such as sphingolipids and sterols—for example, large proteins, such as bacteriorhodopsin, aggregate and create distinct domains.
Another mechanism for membrane domain formation involves membrane proteins interacting with...
3.8K
Rab Proteins01:14

Rab Proteins

5.0K
Rab proteins constitute the largest family of monomeric GTPases, of which 70 members are present in humans. Rab proteins and their effectors regulate consecutive stages of vesicle transport such as vesicle transport, docking, and fusion to the correct recipient membrane.
Rab proteins switch between a cytosolic, GDP-bound inactive state and a membrane-anchored, GTP-bound active state. By themselves, Rabs show slow rates of GDP/GTP exchange and GTP hydrolysis. Thus, Rab proteins are considered...
5.0K
Membrane Domains01:18

Membrane Domains

7.0K
The membrane domains concentrate specific lipids and proteins at one place within the membrane, which helps in cell signaling, adhesion, and other critical cellular processes. These domains can differ in size, composition, function, and lifespan.
Protein Domains
The membrane comprises a group of distinct proteins responsible for carrying out a cell's specific function. For example, the plasma membrane of the human sperm, or a single germ cell, contains a unique set of proteins in the...
7.0K
SNAREs and Membrane Fusion01:43

SNAREs and Membrane Fusion

12.4K
Once a transport vesicle has recognized its target organelle, the vesicular membrane needs to fuse with the target membrane to unload the cargo. Transmembrane proteins called SNAREs present on organelle membranes and their vesicles, mediate vesicle fusion.
SNAREs exist in pairs that symmetrically interact and catalyze the fusion of the lipid bilayers in vesicle and target organelle. v-SNARE in the vesicle membrane are single polypeptide chains that bind to a complementary t-SNARE, composed of 2...
12.4K
Membrane Fluidity01:26

Membrane Fluidity

14.5K
Membrane fluidity is explained by the fluid mosaic model of the cell membrane, which describes the plasma membrane structure as a mosaic of components—including phospholipids, cholesterol, proteins, and carbohydrates—that gives the membrane a fluid character.
Mosaic nature of the membrane
The mosaic characteristic of the membrane helps the plasma membrane remain fluid. The integral proteins and lipids exist as separate but loosely-attached molecules in the membrane. The membrane is...
14.5K
Formation of Lipopolysaccharides01:19

Formation of Lipopolysaccharides

556
Lipopolysaccharides (LPS) are crucial components of the outer membrane of Gram-negative bacteria, serving both structural and functional roles. It contributes to membrane stability and protects bacteria from host immune responses. LPS is composed of three major regions—lipid A, a core oligosaccharide, and an O antigen. The biosynthesis and assembly of LPS involve a highly coordinated set of enzymatic reactions and transport mechanisms. Additionally, LPS is recognized as an endotoxin,...
556

You might also read

Related Articles

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

Sort by
Same author

Polyprolinated Liposomes: Toward Thermoresponsive Shielding and Controlled Release.

Langmuir : the ACS journal of surfaces and colloids·2026
Same author

On-Cell Detection of Polysaccharide One-Bond <sup>1</sup>J<sub>CH</sub> Couplings by Proton-Detected Solid-State NMR.

Journal of the American Chemical Society·2026
Same author

Methicillin treatment reveals that FtsZ phosphorylation influences the cell division of <i>Streptococcus pneumoniae</i>.

PNAS nexus·2026
Same author

Structural dissection of the catalytic domain of the serine threonine kinase StkP of Streptococcus pneumoniae.

Nature communications·2026
Same author

Structures and Dynamics of Tau Assemblies from Solid-State NMR.

Accounts of chemical research·2026
Same author

ATP-driven membrane binding and polymerization of bacterial actin MreB promotes local membrane fluidization.

Biophysical journal·2026

Related Experiment Video

Updated: Jan 18, 2026

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

Structural Basis of the Membrane Association by the Conserved RocS Membrane-Targeting Sequence in Streptococcus.

Ana Álvarez-Mena1, Estelle Morvan2, Clara Lambert3

  • 1Univ. Bordeaux, CNRS, Bordeaux INP, CBMN, UMR 5248, Pessac, France.

Advanced Science (Weinheim, Baden-Wurttemberg, Germany)
|January 16, 2026
PubMed
Summary

The RocS protein

Keywords:
AFMchromosome partitioningmembrane‐protein interactionssolid‐state NMRstreptococcus

More Related Videos

Transmembrane Domain Oligomerization Propensity determined by ToxR Assay
06:45

Transmembrane Domain Oligomerization Propensity determined by ToxR Assay

Published on: May 26, 2011

15.6K
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

Related Experiment Videos

Last Updated: Jan 18, 2026

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
Transmembrane Domain Oligomerization Propensity determined by ToxR Assay
06:45

Transmembrane Domain Oligomerization Propensity determined by ToxR Assay

Published on: May 26, 2011

15.6K
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

Area of Science:

  • Microbiology
  • Molecular Biology
  • Biophysics

Background:

  • Chromosome segregation in *Streptococcus pneumoniae* depends on the membrane protein RocS.
  • RocS links DNA to the cell membrane, but its C-terminal membrane anchor mechanism is unclear.

Purpose of the Study:

  • Investigate the molecular basis of RocS C-terminal membrane targeting.
  • Elucidate the interaction between the RocS anchor and the lipid membrane.

Main Methods:

  • Magic-angle spinning NMR and wide-line NMR spectroscopy.
  • Atomic force microscopy (AFM) imaging.
  • Mutational analysis of the RocS C-terminal region.

Main Results:

  • The RocS anchor forms a kink-helix motif inserted into the membrane, perturbing lipid packing.
  • Membrane fluidity affects anchor-membrane interactions.
  • The anchor associates with lipid nanodomains and forms clusters.
  • A glycine mutation disrupts chromosome segregation and alters membrane properties.

Conclusions:

  • The RocS kink-helix anchor targets specific lipid nanodomains for membrane association.
  • This mechanism is conserved across bacteria, highlighting the anchor's role in membrane targeting.