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Related Concept Videos

Translocation of Proteins into the Mitochondria01:19

Translocation of Proteins into the Mitochondria

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Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
Sorting of outer membrane proteins:
Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...
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Mitochondrial Precursor Proteins01:39

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Mitochondrial precursors are partially unfolded or loosely folded polypeptide chains. Newly synthesized precursors are inhibited from spontaneously folding into their native conformation by the cytosolic chaperones, heat shock proteins 70 (Hsp70), and mitochondrial import stimulation factors (MSFs). Precursors bound to MSFs are guided to the TOM70-TOM37 receptors, while precursors bound to Hsp70  chaperones are targetted to TOM20-TOM22 receptor complexes.
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Measuring Mitochondrial Substrate Flux in Recombinant Perfringolysin O-Permeabilized Cells
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A Selective Fluorogenic Peptide Substrate for the Human Mitochondrial ATP-Dependent Protease Complex ClpXP.

Zhou Sha1, Jennifer Fishovitz2, Susan Wang3

  • 1Department of Chemistry, Case Western Reserve University, Cleveland, Ohio, 44106, USA.

Chembiochem : a European Journal of Chemical Biology
|March 18, 2020
PubMed
Summary

Researchers developed a new fluorogenic peptide substrate to study human ClpXP protease activity. This tool helps investigate the protein quality control functions of human ClpXP (hClpXP) in cells.

Keywords:
AAA+ proteaseEnzymesenzyme kineticshydrolasespeptides

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Protease research

Background:

  • Human mitochondrial matrix ATP-dependent proteases, including human ClpXP (hClpXP) and human Lon (hLon), are crucial for protein quality control.
  • The specific physiological functions of hClpXP remain poorly understood, hindering comprehensive research into its roles.

Purpose of the Study:

  • To differentiate the substrate specificities of hClpXP and hLon.
  • To develop protease-specific peptide substrates as chemical biology tools for investigating hClpXP functions.

Main Methods:

  • Degradation profiling of casein, a decapeptide library, and a known bacterial ClpXP substrate using both hClpXP and hLon.
  • Design and synthesis of a specific fluorogenic peptide substrate (FR-Cleptide) for hClpXP.
  • Utilizing FR-Cleptide to identify inhibitors and detect endogenous protease activity.

Main Results:

  • Characterization of hClpXP and hLon substrate preferences.
  • Successful generation of FR-Cleptide, a specific substrate for hClpXP, with determined kinetic parameters (kcat, Km).
  • Demonstrated utility of FR-Cleptide in identifying a lead inhibitor and detecting hClpXP activity in HeLa cell lysate.

Conclusions:

  • The developed fluorogenic peptide substrate (FR-Cleptide) is an effective tool for monitoring hClpXP activity.
  • This substrate aids in the mechanistic characterization of hClpXP.
  • These peptide-based tools complement existing substrates for hLon, facilitating research into the physiological roles of both proteases.