Penicillium chrysogenum Pex14/17p – a novel component of the peroxisomal membrane that is important for penicillin production

Lukasz Opalinski, Jan A. K. W. Kiel, Tim G. Homan, Marten Veenhuis, Ida J. van der Klei*, Łukasz Opaliński

*Corresponding author for this work

Research output: Contribution to journalArticleAcademicpeer-review

34 Citations (Scopus)

Abstract

By genome analysis, we previously identified Pex14/17p as a putative novel peroxin of Penicillium chrysogenum. Here, we show that Pex14/17p is a component of the peroxisomal membrane that is essential for efficient peroxisomal targeting signal 1 and peroxisomal targeting signal 2 matrix protein import, implying that the protein is indeed a genuine peroxin. Additionally, a PEX14/17 deletion strain is affected in conidiospore formation. Pex14/17p has properties of both Pex14p and Pex17p, in that the N-terminus of this protein is similar to the highly conserved Pex5p-binding region present in the N-termini of Pex14p proteins, whereas its C-terminus shows weak similarity to yeast Pex17p proteins. We have identified a novel motif in both Pex17p and Pex14/17p that is absent in Pex14p. We show that an N-terminally truncated, but not a C-terminally truncated, Pex14/17p is able to complement both the matrix protein import and sporulation defects of a Delta pex14/17 strain, implying that it is the Pex17p-related portion of the protein that is crucial for its function as a peroxin. Possibly, this compensates for the fact that P. chrysogenum lacks an authenthic Pex17p. We also show that, in P. chrysogenum, Pex14/17p plays a role in making the penicillin biosynthesis process more efficient.

Original languageEnglish
Pages (from-to)3203-3218
Number of pages16
JournalFebs Journal
Volume277
Issue number15
DOIs
Publication statusPublished - Aug-2010

Keywords

  • antibiotic production
  • fungi
  • peroxisome
  • protein sorting
  • sporulation
  • YEAST HANSENULA-POLYMORPHA
  • GENE ENCODES
  • COLLETOTRICHUM-LAGENARIUM
  • ASPERGILLUS-NIDULANS
  • PODOSPORA-ANSERINA
  • METABOLIC FUNCTION
  • PROTEIN
  • BIOGENESIS
  • BIOSYNTHESIS
  • MACHINERY

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