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Related Experiment Videos

Hansenula polymorpha Pex14p phosphorylated in vivo.

M Komori1, M Veenhuis

  • 1Laboratory of Molecular Biology, Department of Veterinary Science, Osaka Prefecture University, 1-1 Gakuen-cho, Sakai, Osaka 599-8531, Japan. Komori@vet.osakafu-u.ac.jp

Cell Biochemistry and Biophysics
|May 2, 2001
PubMed
Summary

Hansenula polymorpha Pex14p, a protein vital for peroxisome creation, is phosphorylated in vivo. Its phosphorylation site is located in the C-terminal 58 residues, crucial for peroxisome biogenesis.

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Peroxisomes are essential organelles involved in various metabolic processes.
  • Peroxisome biogenesis is a complex process requiring numerous proteins, including peroxins (Pex).
  • Hansenula polymorpha Pex14p is a newly identified peroxisomal membrane protein crucial for peroxisome assembly.

Purpose of the Study:

  • To investigate the post-translational modification of Hansenula polymorpha Pex14p.
  • To identify the phosphorylation status and site of Pex14p.
  • To understand the role of Pex14p phosphorylation in peroxisome biogenesis.

Main Methods:

  • In vivo labeling of wild-type cells using 32P-orthophosphate.
  • Alkaline phosphatase treatment of labeled Pex14p.

Related Experiment Videos

  • Analysis of phosphoamino acids.
  • Expression of truncated Pex14p variants in a PEX14-deletion strain.

    • Main Results:

    • Hansenula polymorpha Pex14p is phosphorylated in vivo.
    • The major phosphoamino acid in Pex14p is acid-labile.
    • Phosphorylation of Pex14p occurs within its C-terminal 58 residues.

    Conclusions:

    • Pex14p is a phosphoprotein essential for peroxisome biogenesis in Hansenula polymorpha.
    • The C-terminal region of Pex14p contains the phosphorylation site(s).
    • Understanding Pex14p phosphorylation provides insights into the regulation of peroxisome assembly.