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Related Experiment Videos

A novel C3-like ADP-ribosyltransferase from Staphylococcus aureus modifying RhoE and Rnd3.

C Wilde1, G S Chhatwal, G Schmalzing

  • 1Institut für Experimentelle und Klinische Pharmakologie und Toxikologie der Universität Freiburg, Hermann-Herder-Strasse 5, D-79104 Freiburg, Germany.

The Journal of Biological Chemistry
|January 2, 2001
PubMed
Summary

A new Staphylococcus aureus C3-like transferase, C3(Stau), modifies RhoE and Rnd3, unlike other C3 enzymes. This discovery expands the C3 transferase family and identifies a novel RhoE/Rnd modifying subfamily.

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Area of Science:

  • Microbiology
  • Molecular Biology
  • Cell Biology

Background:

  • Clostridium botulinum C3 transferase targets RhoA, RhoB, and RhoC, inactivating them via ADP-ribosylation at Asn-41, leading to actin cytoskeleton disruption.
  • C3-like transferases are a family of enzymes known for their specific ADP-ribosylation activity on Rho GTPases.

Purpose of the Study:

  • To identify and characterize a novel C3-like transferase from a pathogenic Staphylococcus aureus strain.
  • To determine the substrate specificity and in vivo activity of the newly identified transferase, C3(Stau).
  • To investigate the potential of C3(Stau) in altering cellular morphology and cytoskeleton.

Main Methods:

  • Cloning of the C3(Stau) transferase from Staphylococcus aureus genomic DNA.
  • Recombinant protein expression and characterization of substrate specificity using Rho proteins.

Related Experiment Videos

  • In vivo validation of substrate modification in Xenopus laevis oocytes.
  • Construction of a chimeric toxin to enhance cell accessibility and observe cytoskeletal effects.

    • Main Results:

    • The novel C3(Stau) transferase was cloned and characterized, showing 35% amino acid identity to other C3 enzymes.
    • C3(Stau) uniquely modifies RhoE and Rnd3 at Asn-44, in addition to RhoA, unlike other C3 transferases.
    • In vivo studies confirmed RhoE modification by C3(Stau), and a chimeric C3(Stau) induced cytoskeletal changes similar to C. botulinum C3.
    • RhoE and Rnd3 are Rho subfamily members with low intrinsic GTPase activity and antagonistic functions to RhoA.

    Conclusions:

    • C3(Stau) represents a new member of the C3-like transferase family.
    • It is the prototype of a novel subfamily of RhoE/Rnd modifying transferases.
    • The findings expand the known targets of C3-like enzymes and provide insights into their cellular functions.