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Self-cleaving proteases.

W S Blair1, B L Semler

  • 1University of California, Irvine.

Current Opinion in Cell Biology
|December 1, 1991
PubMed
Summary
This summary is machine-generated.

Self-cleaving proteases regulate diverse systems in bacteria, mammals, and viruses. This review details intramolecular cleavage of LexA in E. coli, pepsinogen activation in mammals, and picornavirus polyprotein processing.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Background:

  • Self-cleaving proteases play crucial roles in cellular regulation.
  • Protein processing is a key mechanism for controlling biological functions.
  • Understanding these proteases offers insights into various biological systems.

Purpose of the Study:

  • To review the activity of self-cleaving proteases.
  • To emphasize the diversity of regulatory systems controlled by protein processing.
  • To examine specific examples in bacterial, mammalian, and viral systems.

Main Methods:

  • Literature review focusing on protein processing and self-cleaving proteases.
  • Analysis of regulatory systems involving intramolecular cleavage.
  • Case studies of specific protease activities.

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Main Results:

  • RecA-dependent intramolecular cleavage of Escherichia coli LexA protein.
  • Intramolecular activation of mammalian aspartic acid protease, pepsinogen.
  • Autocatalytic cleavage of polyproteins synthesized by picornaviruses.

Conclusions:

  • Self-cleaving proteases exhibit diverse mechanisms across different organisms.
  • Protein processing is a fundamental regulatory strategy in biology.
  • These proteases are essential for cellular functions and pathogen replication.