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Penicillium chrysogenum Pex14/17p – a novel component of the peroxisomal membrane that is important for penicillin production
Author(s) -
Opaliński Łukasz,
Kiel Jan A. K. W.,
Homan Tim G.,
Veenhuis Marten,
van der Klei Ida J.
Publication year - 2010
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/j.1742-4658.2010.07726.x
Subject(s) - penicillium chrysogenum , peroxisomal targeting signal , biology , peroxisome , biochemistry , gene
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 Δ 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.