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

Directing Proteins to the Rough Endoplasmic Reticulum01:34

Directing Proteins to the Rough Endoplasmic Reticulum

7.1K
The organelle-specific signaling sequences direct proteins synthesized in the cytosol to their final destination like ER, mitochondria, peroxisomes, etc. Some of the proteins directed to ER are then trafficked via vesicles to other organelles within the cell or the extracellular environment through the Golgi complex. For example, the rough ER synthesizes soluble proteins for transportation to the lysosomes or secretion out of the cell. It can also synthesize transmembrane proteins that can...
7.1K
Regulation of the Unfolded Protein Response01:31

Regulation of the Unfolded Protein Response

2.4K
Inositol-requiring kinase one or IRE1 is the most conserved eukaryotic unfolded protein response (UPR) receptor. It is a type I transmembrane protein kinase receptor with a distinctive site-specific RNase activity. As the binding mechanics of the misfolded proteins with the N-terminal domain of IRE-1 are unclear, three binding models — direct, indirect, and allosteric -- are proposed for receptor activation. Nevertheless, it is known that once a misfolded protein associates with IRE1, it...
2.4K
Export of Misfolded Proteins out of the ER01:32

Export of Misfolded Proteins out of the ER

3.5K
After folding, the ER assesses the quality of secretory and membrane proteins. The correctly folded proteins are cleared by the calnexin cycle for transport to their final destination, while misfolded proteins are held back in the ER lumen. The ER chaperones attempt to unfold and refold the misfolded proteins but sometimes fail to achieve the correct native conformation. Such terminally misfolded proteins are then exported to the cytosol by ER-associated degradation or ERAD pathway for...
3.5K
Conservative Site-specific Recombination and Phase Variation02:53

Conservative Site-specific Recombination and Phase Variation

5.9K
Because the DNA segments are cut and reorganized in a direction-specific manner, site-specific recombination has emerged as an efficient genetic engineering technique. Flippase and Cyclization recombinases or Flp and Cre, respectively, are two members of the tyrosine recombinase family derived from bacteriophages, that are used to mediate site-specific DNA insertions, deletions, and targeted expression of proteins in mammalian cell lines.
The recognition sites for Cre recombinase called LoxP...
5.9K
Protein Folding Quality Check in the RER01:29

Protein Folding Quality Check in the RER

3.7K
ER is the primary site for the maturation and folding of soluble and transmembrane secretory proteins. The calnexin cycle is a specific chaperone system that folds and assesses the confirmation of N-glycosylated proteins before they can exit the ER lumen. The primary players of this quality check pipeline are the lectins, ER-resident chaperones, and a glucosyl transferase enzyme. In case the calnexin system in the lumen fails to salvage a misfolded protein, it is transported to the cytoplasm...
3.7K

You might also read

Related Articles

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

Sort by
Same author

A Simple and Cost-Effective Electrochemical Assay for Heart Failure Prognosis Using Soluble Suppression of Tumorigenicity 2‑Specific Nanobodies.

ACS pharmacology & translational science·2026
Same author

The penicillin-binding protein PBP1b fortifies the Escherichia coli division site against osmotic rupture.

Nature microbiology·2026
Same author

Zero-shot design of drug-binding proteins via neural iterative selection-expansion.

Nature·2026
Same author

Secretin-interacting plug proteins prevent antibiotic influx during type IV pilus assembly in Pseudomonas aeruginosa.

Nature communications·2026
Same author

<i>De novo</i> design of transmembrane accessory subunits for fold stabilization and expansion.

bioRxiv : the preprint server for biology·2026
Same author

In silico discovery of nanobody binders to a G-protein coupled receptor using AlphaFold-Multimer.

Nature communications·2026

Related Experiment Video

Updated: Jun 10, 2025

Author Spotlight: Exploring Cellular Processes by Modeling Ligands in Cryo-EM Maps
09:30

Author Spotlight: Exploring Cellular Processes by Modeling Ligands in Cryo-EM Maps

Published on: July 19, 2024

1.2K

MreC-MreD structure reveals a multifaceted interface that controls MreC conformation.

Morgan S A Gilman1, Irina Shlosman1, Daniel D Samé Guerra1

  • 1Department of Biological Chemistry and Molecular Pharmacology, Blavatnik Institute, Harvard Medical School, Boston, Massachusetts 02115, USA.

Biorxiv : the Preprint Server for Biology
|October 17, 2024
PubMed
Summary

MreD regulates bacterial cell wall synthesis by controlling the conformation of MreC within the Rod complex. This interaction is crucial for bacterial growth and presents a potential antibiotic target.

More Related Videos

Stability and Structure of Bat Major Histocompatibility Complex Class I with Heterologous &#946;2-Microglobulin
11:17

Stability and Structure of Bat Major Histocompatibility Complex Class I with Heterologous β2-Microglobulin

Published on: March 10, 2021

6.4K
Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR
14:44

Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR

Published on: December 16, 2013

9.6K

Related Experiment Videos

Last Updated: Jun 10, 2025

Author Spotlight: Exploring Cellular Processes by Modeling Ligands in Cryo-EM Maps
09:30

Author Spotlight: Exploring Cellular Processes by Modeling Ligands in Cryo-EM Maps

Published on: July 19, 2024

1.2K
Stability and Structure of Bat Major Histocompatibility Complex Class I with Heterologous &#946;2-Microglobulin
11:17

Stability and Structure of Bat Major Histocompatibility Complex Class I with Heterologous β2-Microglobulin

Published on: March 10, 2021

6.4K
Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR
14:44

Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR

Published on: December 16, 2013

9.6K

Area of Science:

  • Microbiology
  • Structural Biology
  • Molecular Biology

Background:

  • The peptidoglycan (PG) cell wall is essential for bacterial survival and is a key antibiotic target.
  • MreD is an accessory factor of the Rod complex, responsible for PG synthesis during cell elongation, but its mechanism is poorly understood.

Purpose of the Study:

  • To elucidate the structural and functional role of MreD in the bacterial Rod complex.
  • To understand how MreD facilitates peptidoglycan synthesis and bacterial cell shape determination.

Main Methods:

  • Determined the cryo-electron microscopy structure of *Thermus thermophilus* MreD in complex with MreC.
  • Utilized single-molecule Förster Resonance Energy Transfer (FRET) to analyze MreD-MreC interactions and conformational changes.
  • Investigated the in vivo effects of disrupting MreD-MreC interactions in *E. coli*.

Main Results:

  • The cryo-EM structure revealed a specific interaction between a pocket on MreD and membrane-proximal regions of MreC.
  • Single-molecule FRET demonstrated that MreD induces a specific conformation in MreC, priming it for Rod complex activation.
  • Disruption of these MreD-MreC interactions in *E. coli* led to the abolition of Rod complex activity in vivo.

Conclusions:

  • MreD plays a critical role in regulating bacterial cell shape by controlling MreC conformation within the Rod complex.
  • The identified MreD-MreC interaction is essential for peptidoglycan synthesis and bacterial cell integrity.
  • MreD represents a potential novel antibiotic target due to its crucial role in bacterial cell wall maintenance.