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

Does a bacterial elongation factor share a common evolutionary ancestor with actin?

J P Rosenbusch, G R Jacobson, J C Jaton

    Journal of Supramolecular Structure
    |January 1, 1976
    PubMed
    Summary

    Protein synthesis elongation factor Tu (EF-Tu) from E. coli shares properties with actin. Limited tryptic degradation suggests similar molecular architecture, hinting at a possible common evolutionary origin for EF-Tu and actin-like proteins.

    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

    A novel concept of membrane reconstitution applied to acetylcholine receptor from Torpedo and matrix protein from escherichia coli.

    Neurochemistry international·2010
    Same author

    Three Dimensional Structure of a Membrane Pore: Electron Microscopical Analysis of Escherichia coli Outer Membrane Matrix Porin.

    Biophysical journal·2009
    Same author

    Stability of membrane proteins: relevance for the selection of appropriate methods for high-resolution structure determinations.

    Journal of structural biology·2002
    Same author

    Molecular mechanism for the crystallization of bacteriorhodopsin in lipidic cubic phases.

    FEBS letters·2001
    Same author

    High-resolution structures and dynamics of membrane protein--lipid complexes: a critique.

    Current opinion in structural biology·2001
    Same author

    Role of charged residues at the OmpF porin channel constriction probed by mutagenesis and simulation.

    Biochemistry·2001

    Area of Science:

    • Molecular Biology
    • Biochemistry
    • Evolutionary Biology

    Background:

    • Protein synthesis elongation factor Tu (EF-Tu) from Escherichia coli exhibits similarities to actin-like proteins.
    • These similarities extend to physical, chemical, and functional characteristics.

    Purpose of the Study:

    • To investigate the structural and evolutionary relationship between EF-Tu and actin-like proteins.
    • To present initial findings supporting a potential common ancestry.

    Main Methods:

    • Comparative analysis of physical, chemical, and functional properties.
    • Limited tryptic degradation to assess molecular architecture.

    Main Results:

    • EF-Tu and actin-like proteins share significant physical, chemical, and functional properties.

    Related Experiment Videos

  • Limited tryptic degradation revealed a similar molecular architecture between EF-Tu and actin-like proteins.
  • Conclusions:

    • The observed similarities suggest a possible evolutionary link between EF-Tu and actin-like proteins.
    • Further research is required to definitively establish or refute this evolutionary hypothesis.