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Related Experiment Videos

Cytochrome c methylation.

W K Paik1, Y B Cho, B Frost

  • 1Fels Institute for Cancer Research and Molecular Biology, Temple University School of Medicine, Philadelphia, PA 19140.

Biochemistry and Cell Biology = Biochimie Et Biologie Cellulaire
|September 1, 1989
PubMed
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Protein methylation, particularly of cytochrome c, is explored. Methylation at Lys-77 influences mitochondrial import preference in yeast by altering physicochemical properties.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Post-translational Modifications

Background:

  • Protein methylation is a crucial post-translational modification affecting protein function.
  • Cytochrome c methylation, specifically at Lys-77 in lower eukaryotes, serves as a model system for studying this process.
  • Early research established that cytochrome c methylation occurs post-translationally before mitochondrial import.

Purpose of the Study:

  • To review general aspects of protein methylation, focusing on cytochrome c methylation.
  • To investigate the role of Lys-77 methylation in cytochrome c's interaction with mitochondria.
  • To elucidate the biophysical consequences of methylation on apocytochrome c and its import mechanism.

Main Methods:

  • Purification and characterization of the methyltransferase enzyme.

Related Experiment Videos

  • In vitro methylation assays using purified proteins and in vitro translated apocytochrome c.
  • Mitochondrial import studies using isolated yeast and rat liver mitochondria.
  • Analysis of physicochemical properties, including isoelectric point and Stokes radius.

    • Main Results:

    • Methylation of apocytochrome c occurs specifically at Lys-77.
    • Methylated apocytochrome c shows preferential import into yeast mitochondria, unlike rat liver mitochondria.
    • Methylation significantly decreases the isoelectric point and Stokes radius of apocytochrome c.

    Conclusions:

    • Cytochrome c methylation at Lys-77 is a key regulatory mechanism influencing mitochondrial targeting in certain organisms.
    • The observed changes in isoelectric point and Stokes radius suggest a disruption of hydrogen bonds, potentially explaining altered import.
    • This modification highlights the diverse roles of protein methylation in cellular processes and warrants further investigation into its in vivo significance.