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Related Experiment Videos

Post-translational arginylation and intracellular proteolysis.

P Bohley1, J Kopitz, G Adam

  • 1Physiologisch-chemisches Institut, Eberhard-Karls-Universität, Tübingen, Germany.

Biomedica Biochimica Acta
|January 1, 1991
PubMed
Summary

Cellular proteins are degraded faster when tagged with arginine through post-translational arginylation. This process, involving arginyl transferase, targets proteins like ornithine decarboxylase (ODC) for rapid breakdown by proteinases.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Background:

  • Cellular proteins can be targeted for degradation via N-terminal amino acids.
  • N-terminal arginine residues are known to destabilize cytosolic proteins.

Purpose of the Study:

  • To investigate the post-translational arginylation of cytosolic proteins, particularly ornithine decarboxylase (ODC).
  • To determine the role of arginyl transferase in protein degradation.
  • To explore the reversibility and scope of protein arginylation.

Main Methods:

  • Incubation with radioactive L-arginyl-tRNA to study arginylation.
  • Isolation of ODC using a monoclonal antibody.
  • Edman degradation to identify the site of arginylation.
  • Use of an arginyltransferase inhibitor (L-Glutamyl-L-Valyl-L-Phenylalanine) in cultured hepatocytes.

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Main Results:

  • Post-translational arginylation occurred specifically at the N-terminus of ODC.
  • Arginylated ODC showed significantly higher radioactivity compared to bulk cytosolic proteins.
  • Inhibition of arginyltransferase increased ODC half-life in hepatocytes.
  • At least 25 cytosolic proteins in hepatocytes and 15 in Dictyostelium discoideum can be arginylated.
  • Arginylated proteins are degraded more rapidly by cellular proteinases, especially calpains.

Conclusions:

  • Post-translational arginylation by arginyl transferase targets cytosolic proteins, including ODC, for accelerated degradation.
  • This arginylation process is reversible and affects a wide range of cytosolic proteins.
  • The study highlights a key mechanism regulating protein turnover and cellular proteostasis.