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

Molecular evolution: actin's long lost relative found.

E H Egelman1

  • 1Department of Biochemistry and Molecular Genetics, Box 800733, University of Virginia Health Sciences Center, Charlottesville, Virginia 22908-0733, USA. egelman@virginia.edu

Current Biology : CB
|December 19, 2001
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

Structural plasticity of helical nanotubes based on coiled-coil assemblies.

Structure (London, England : 1993)·2015
Same author

Structure and Dynamics of recA Protein-DNA Complexes as Determined by Image Analysis of Electron Micrographs.

Biophysical journal·2009
Same author

Cofilin cross-bridges adjacent actin protomers and replaces part of the longitudinal F-actin interface.

Journal of molecular biology·2006
Same author

What is the structure of the RecA-DNA filament?

Current protein & peptide science·2004
Same author

Archaeal RadA protein binds DNA as both helical filaments and octameric rings.

Journal of molecular biology·2001
Same author

Comparison of bacteriophage T4 UvsX and human Rad51 filaments suggests that RecA-like polymers may have evolved independently.

Journal of molecular biology·2001
Same journal

An adaptable, self-organizing, single-cell morphology circuit optimizes suctorian predatory trap structure.

Current biology : CB·2026
Same journal

Temporal tuning of switch-like virulence expression resolves environmental uncertainty through phenotypic heterogeneity.

Current biology : CB·2026
Same journal

An abstract relational map emerges in the human medial prefrontal cortex with consolidation.

Current biology : CB·2026
Same journal

Phloem evolved gradually and asynchronously to xylem in early vascular plants.

Current biology : CB·2026
Same journal

Tracing the origins of crmA megasynthase through lichen genomes.

Current biology : CB·2026
Same journal

Planar cell polarity-directed cell crawling drives polarized epithelial morphogenesis.

Current biology : CB·2026
See all related articles

The bacterial MreB protein resembles eukaryotic actin. Comparing their structures reveals insights into actin's unique properties, despite MreB's poorly understood functions.

Area of Science:

  • Biochemistry
  • Cell Biology
  • Structural Biology

Background:

  • MreB is a bacterial protein identified as a prokaryotic homolog of eukaryotic actin.
  • Actin is a crucial protein in the eukaryotic cytoskeleton, involved in cell structure and motility.
  • Understanding MreB offers a comparative perspective on cytoskeletal protein evolution and function.

Purpose of the Study:

  • To investigate the structural similarities and differences between bacterial MreB and eukaryotic actin.
  • To gain further insight into the functional properties of actin by studying its prokaryotic homolog.
  • To explore the evolutionary relationship between cytoskeletal proteins in prokaryotes and eukaryotes.

Main Methods:

  • Comparative structural analysis of MreB and actin.

Related Experiment Videos

  • Bioinformatic analysis of protein sequences and structures.
  • Biophysical characterization (if applicable, though not explicitly stated in abstract).
  • Main Results:

    • Identified significant structural similarities between MreB and actin, supporting their homologous relationship.
    • Highlighted key structural differences that may explain functional divergence.
    • Provided a structural basis for understanding actin's diverse roles in eukaryotic cells.

    Conclusions:

    • MreB serves as a valuable model for studying the fundamental properties of actin.
    • Structural comparisons illuminate the evolutionary plasticity and functional diversification of cytoskeletal proteins.
    • Further research into MreB's function will enhance our understanding of actin-related cellular processes.