Hansenula polymorpha Pex20p is an oligomer that binds the peroxisomal targeting signal 2 (PTS2)

Marleen Otzen, Dongyuan Wang, Marcel G. J. Lunenborg, Ida J. van der Klei

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Abstract

We have cloned and characterized the Hansenula polymorpha PEX20 gene. The HpPEX20 gene encodes a protein of 309 amino acids (HpPex20p) with a calculated molecular mass of similar to 35 kDa. In cells of an HpPEX20 disruption strain, PTS2 proteins were mislocalized to the cytosol, whereas PTS1 matrix protein import proceeded normally. Also, the PTS2 proteins amine oxidase and thiolase were normally assembled and active in these cells, suggesting HpPex20p is not involved in oligomerization/activation of these proteins. Localization studies revealed that HpPex20p is predominantly associated with peroxisomes. Using fluorescence correlation spectroscopy we determined the native molecular mass of purified HpPex20p and binding of a synthetic peptide containing a PTS2 sequence. The data revealed that purified HpPex20p forms oligomers, which specifically bind PTS2-containing peptides.

Original languageEnglish
Pages (from-to)3409-3418
Number of pages10
JournalJournal of Cell Science
Volume118
Issue number15
DOIs
Publication statusPublished - 1-Aug-2005

Keywords

  • yeast
  • PTS2 protein import
  • peroxisomes
  • FCS
  • Hansenula polymorpha
  • TARGETING SIGNAL RECEPTOR
  • YEAST YARROWIA-LIPOLYTICA
  • SACCHAROMYCES-CEREVISIAE
  • PROTEIN IMPORT
  • PEROXISOME BIOGENESIS
  • CORRELATION SPECTROSCOPY
  • ALCOHOL OXIDASE
  • MATRIX PROTEIN
  • PEX5P
  • PEX18P

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