Related Experiment Video

Updated: Jun 27, 2026

SNARE-mediated Fusion of Single Proteoliposomes with Tethered Supported Bilayers in a Microfluidic Flow Cell Monitored by Polarized TIRF Microscopy
10:58

SNARE-mediated Fusion of Single Proteoliposomes with Tethered Supported Bilayers in a Microfluidic Flow Cell Monitored by Polarized TIRF Microscopy

Published on: August 24, 2016

Structural and functional diversity of bacterial membrane fusion proteins

Helen I Zgurskaya1, Yoichi Yamada, Elena B Tikhonova

  • 1University of Oklahoma Department of Chemistry and Biochemistry 620 Parrington Oval, Room 208 Norman, OK 73019, USA. elenaz@ou.edu

Biochimica Et Biophysica Acta
|December 2, 2008
PubMed

Insights

Membrane fusion proteins (MFPs) are crucial for bacterial transport systems. This review explores MFP diversity, structure, and mechanisms, revealing their roles in multidrug efflux across bacterial types.

Area of Science:

  • Microbiology
  • Molecular Biology
  • Biochemistry

Background:

  • Membrane fusion proteins (MFPs) are vital components of bacterial multi-component transporters.
  • They are associated with Resistance-Nodulation-cell Division (RND), ATP-Binding Cassette (ABC), and Major Facilitator (MF) superfamilies.
  • MFPs are increasingly recognized for their active role in substrate interaction and transport reactions.

Purpose of the Study:

  • To review the diversity, structure, and molecular mechanisms of MFPs involved in multidrug efflux.
  • To analyze the representation of multidrug MFPs in bacterial genomes using phylogenetic approaches.
  • To identify and characterize MFPs in Gram-positive bacteria.

Main Methods:

  • Phylogenetic analysis of sequenced bacterial genomes.
  • Sequence analysis of identified MFPs.
  • Review of current literature on MFP structure and function.

Main Results:

  • Identified MFPs associated with RND-, MF-, and ABC-type transporters in Gram-positive bacteria, expanding known MFP diversity.
  • MFPs exhibit significant size variation (200-650 amino acids) and some lack the characteristic alpha-helical domain.
  • Many bacterial transport operons encode multiple distinct MFPs.

Conclusions:

  • MFPs display considerable diversity in Gram-positive bacteria, challenging previous classifications.
  • Understanding MFP diversity is key to elucidating the structure and mechanism of MFP-dependent transporters.
  • This review provides a comprehensive overview of MFPs in multidrug efflux systems.

More Related Videos

A Model Membrane Platform for Reconstituting Mitochondrial Membrane Dynamics10:31

A Model Membrane Platform for Reconstituting Mitochondrial Membrane Dynamics

Published on: September 2, 2020

Detergent-free Ultrafast Reconstitution of Membrane Proteins into Lipid Bilayers Using Fusogenic Complementary-charged Proteoliposomes.11:10

Detergent-free Ultrafast Reconstitution of Membrane Proteins into Lipid Bilayers Using Fusogenic Complementary-charged Proteoliposomes.

Published on: April 5, 2018

Related Concept Videos

SNAREs and Membrane Fusion01:43

SNAREs and Membrane Fusion

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

Multi-pass Transmembrane Proteins and β-barrels

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 G-protein-linked receptors (GPCRs) and...
Cytoskeletal Proteins in Bacteria01:29

Cytoskeletal Proteins in Bacteria

Bacterial cells were initially considered simple, randomly organized structures lacking a cytoskeleton. However, the discovery of cytoskeleton homologs in bacteria led to the change of this opinion. Bacterial cytoskeletal filaments regulate the cell shape, cell polarity, cell division, and partitioning of plasmids during cell division. It was later discovered that bacterial cytoskeletal proteins, mainly actin and tubulin homologs, are diverse compared to their eukaryotic counterparts. On the...
Fusion of Secretory Vesicles with the Plasma Membrane01:26

Fusion of Secretory Vesicles with the Plasma Membrane

Proteins and neurotransmitters in secretory vesicles can be released from a cell upon vesicle docking, priming, and fusion with the plasma membrane. Vesicles are docked and primed in preparation for the quick exocytosis of their contents in response to a stimulus. The fusion process is mainly carried out by a SNAP Receptor or SNARE complex, consisting of synaptobrevin, syntaxin-1, and SNAP-25.
In 1993, Jim Rothman proposed that the antiparallel pairing of vesicular and transmembrane SNAREs, or...
Mechanisms of Membrane Domain Formation00:59

Mechanisms of Membrane Domain Formation

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 cytoskeletal...
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...