The first direct activity assay for the mitochondrial protease OMA1

Mitochondrion. 2019 May;46:1-5. doi: 10.1016/j.mito.2019.03.001. Epub 2019 Mar 26.

Abstract

Mitochondria continually undergo fission and fusion which allow mitochondria to rapidly change their shape, size, and function throughout the cell life cycle. OMA1, a zinc metalloproteinase enzyme, is a key regulator of the mitochondrial fusion machinery. The paucity of information regarding OMA1 regulation and function largely stems from the fact that there is no direct method to quantitatively measure its activity. Using a fluorescence-based reporter assay, we developed a sensitive method to measure OMA1 enzymatic activity in whole cell lysates.

Keywords: Fluorescence-based reporter; Fusion; Mitochondria; OMA1; Proteases.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Fluorometry / methods*
  • Humans
  • Metalloendopeptidases / analysis*
  • Mitochondrial Proteins / analysis*

Substances

  • Mitochondrial Proteins
  • Metalloendopeptidases
  • molecule metalloprotease-related protein-1, human