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The peroxisomal membrane protein Pex14p of Hansenula polymorpha is phosphorylated in vivo
Author(s) -
Komori Masayuki,
Kiel Jan A.K.W.,
Veenhuis Marten
Publication year - 1999
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(99)01087-x
Subject(s) - peroxisome , biochemistry , phosphorylation , in vivo , chemistry , phosphatase , biogenesis , biology , microbiology and biotechnology , gene
Hansenula polymorpha Pex14p (HpPex14p) is a component of the peroxisomal membrane essential for peroxisome biogenesis. Here, we show that HpPex14p is phosphorylated in vivo. In wild‐type H. polymorpha cells, grown in the presence of [ 32 P]orthophosphate, the 32 P label was incorporated into HpPex14p. Labelled HpPex14p was induced after a shift of cells to methanol‐containing media and rapidly disappeared after a shift to glucose medium, which induces specific peroxisome degradation. Alkaline phosphatase treatment of labelled HpPex14p resulted in the release of 32 P and a minor shift of the HpPex14p band on Western blots. Phosphoamino acid analysis by two dimensional silica gel thin layer chromatography suggested that the major phosphoamino acid in phosphorylated HpPex14p was acid‐labile.