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Related Experiment Videos

Synthesis, processing, and localization of human Lon protease

N Wang1, M R Maurizi, L Emmert-Buck

  • 1Laboratory of Cell Biology, NCI, National Institutes of Health, Bethesda, Maryland 20892.

The Journal of Biological Chemistry
|November 18, 1994
PubMed
Summary

Human Lon protease, an ATP-dependent protease, is synthesized as a precursor and matures within mitochondria. Its processing requires mitochondrial inner membrane potential and occurs rapidly, with the mature form being stable.

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Area of Science:

  • Mitochondrial Biology
  • Protease Function
  • Cellular Protein Maturation

Background:

  • The bacterial ATP-dependent Lon protease has a conserved homolog in humans.
  • Understanding the synthesis, maturation, and localization of human Lon protease is crucial for mitochondrial function.
  • Previous studies have not fully elucidated the specific pathway for human Lon protease maturation.

Purpose of the Study:

  • To investigate the synthesis, maturation, and subcellular localization of human Lon protease.
  • To determine the role of mitochondrial inner membrane potential in human Lon protease maturation.
  • To characterize the kinetics of human Lon protease precursor processing and mature protein stability.

Main Methods:

  • Immunofluorescence microscopy of transfected cells expressing human Lon protease-FLAG.

Related Experiment Videos

  • In vitro transcription/translation followed by incubation with isolated rat liver mitochondria.
  • Treatment with 2,4-dinitrophenol (DNP) to disrupt mitochondrial membrane potential.
  • Pulse-chase experiments and submitochondrial fractionation.

    • Main Results:

    • Human Lon protease is localized to the mitochondria, specifically the matrix.
    • The protease is synthesized as a ~107 kDa precursor, which is processed to a ~100 kDa mature form within mitochondria.
    • Maturation is dependent on mitochondrial inner membrane potential; disruption by DNP halts processing.
    • The precursor is rapidly converted to the mature form (<2 min half-time) and the mature protease is stable.

    Conclusions:

    • Human Lon protease maturation occurs post-translationally within the mitochondrial matrix.
    • Mitochondrial inner membrane potential is essential for the proteolytic cleavage of human Lon protease.
    • The maturation pathway for human Lon protease is analogous to other mitochondrial matrix proteins.