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Related Experiment Videos

Substrate recognition through a PDZ domain in tail-specific protease.

K D Beebe1, J Shin, J Peng

  • 1Ohio State Biochemistry Program and Department of Chemistry, The Ohio State University, 100 West 18th Avenue, Columbus, Ohio 43210, USA.

Biochemistry
|March 15, 2000
PubMed
Summary

Tail-specific protease (Tsp) uses its PDZ domain to recognize and bind nonpolar C-termini of proteins, enabling selective degradation. This PDZ domain is crucial for Tsp

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Enzymology

Background:

  • Tail-specific protease (Tsp) is a periplasmic enzyme.
  • Tsp selectively degrades proteins with nonpolar C-termini.
  • Substrate specificity suggests a distinct recognition domain separate from the catalytic site.

Purpose of the Study:

  • To identify the substrate recognition domain of Tsp.
  • To elucidate the mechanism of Tsp's selective protein degradation.
  • To characterize the role of the PDZ domain in Tsp function.

Main Methods:

  • Partial proteolysis using V8 protease.
  • Photoaffinity labeling with fluorescent nonpolar peptides.
  • Systematic deletion mutagenesis and site-directed mutagenesis.

Related Experiment Videos

  • Biochemical characterization of the isolated PDZ domain.

    • Main Results:

    • Substrate recognition is mediated by a PDZ domain (amino acids 217-301).
    • The isolated PDZ domain binds nonpolar peptides with high affinity (K(D) = 1.9 microM).
    • Mutagenesis of V229 in the PDZ domain affects substrate binding (K(M)) but not catalysis (k(cat)).

    Conclusions:

    • Tsp utilizes a PDZ domain for selective recognition of nonpolar C-terminal protein sequences.
    • The PDZ domain functions independently in substrate binding.
    • PDZ domains may represent a general mechanism for achieving selective protein degradation.