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 Experiment Videos

Bacterial actin MreB forms antiparallel double filaments.

Fusinita van den Ent1, Thierry Izoré2, Tanmay Am Bharat2

  • 1Structural Studies Division, Medical Research Council - Laboratory of Molecular Biology, Cambridge, United Kingdom fent@mrc-lmb.cam.ac.uk.

Elife
|May 21, 2014
PubMed
Summary
This summary is machine-generated.

Related Concept Videos

You might also read

Related Articles

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

Sort by
Same author

Molecular structure of the ESCRT-III-based archaeal CdvAB cell division machinery.

Proceedings of the National Academy of Sciences of the United States of America·2026
Same author

Cholinergic modulation of hippocampal CA1 pyramidal cell excitability in Arx<sup>GCG+7</sup> mice.

Experimental neurology·2025
Same author

CD33 and clusterin interact biophysically and genetically to modulate Alzheimer risk.

bioRxiv : the preprint server for biology·2025
Same author

Foam film vitrification for cryo-EM.

Nature communications·2025
Same author

Prevalence of Esophageal Webs in Patients Undergoing Direct Laryngoscopy.

The Laryngoscope·2025
Same author

Mechanism of DNA capture by the MukBEF SMC complex and its inhibition by a viral DNA mimic.

Cell·2025
Same journal

SqueakPose Studio, an end-to-end platform for pose estimation and real-time edge-AI deployment.

eLife·2026
Same journal

Mechanistic insights into transcriptional regulation of ARHGAP36 expression identify a factor predictive of neuroblastoma survival.

eLife·2026
Same journal

Activity-dependent CO<sub>2</sub> production in the axon triggers opening of Connexin32 in the Schwann cell paranode.

eLife·2026
Same journal

Lipid packing contributes to the confinement of caveolae to the plasma membrane.

eLife·2026
Same journal

A coma pattern-based autofocusing method resolves bacterial cold shock response at single-cell level.

eLife·2026
Same journal

Non-canonical amino acid incorporation enables minimally disruptive labeling of stress granule and TDP-43 proteinopathy.

eLife·2026
See all related articles

Prokaryotic actin MreB forms antiparallel protofilament pairs, unlike other actin-like proteins. This unique structure is crucial for bacterial cell shape maintenance and is targeted by antimicrobial agents.

Area of Science:

  • Cellular Biology
  • Microbiology
  • Biochemistry

Background:

  • Actin-like proteins typically form parallel protofilaments, establishing cellular polarity.
  • The bacterial actin homologue MreB is essential for maintaining bacterial cell shape.

Purpose of the Study:

  • To investigate the in vitro and in vivo assembly of MreB protofilaments.
  • To elucidate the structural basis of MreB's role in cell shape maintenance.
  • To understand the mechanism of action of MreB-targeting antimicrobial agents.

Main Methods:

  • X-ray crystallography to determine atomic structures of MreB protofilaments.
  • 3D cryo-electron microscopy (cryo-EM) to visualize MreB-membrane interactions.
  • In vivo site-specific cross-linking to confirm protofilament orientation in E. coli.
Keywords:
Caulobacter crescentusThermotoga maritimabacteria

Related Experiment Videos

Main Results:

  • MreB forms antiparallel protofilament pairs in vitro and in vivo, a novel arrangement for actin-like proteins.
  • Antiparallel protofilament doublets are essential for MreB's function in cell shape maintenance.
  • Crystal structures reveal conformational changes associated with antiparallel filament formation.
  • Antimicrobial agents A22/MP265 bind to MreB near the nucleotide, inhibiting hydrolysis and destabilizing protofilament doublets.

Conclusions:

  • Bacterial actin MreB exhibits an atypical antiparallel protofilament assembly.
  • This unique structure is critical for bacterial morphogenesis and represents a target for novel antimicrobials.