The peroxisomal membrane protein Pex14p of Hansenula polymorpha is phosphorylated in vivo

FEBS Letters

Kiel, Jan A.K.W.¹  Komori, Masayuki²  Veenhuis, Marten¹ 

[1] Laboratory of Eukaryotic Microbiology, Groningen Biomolecular Sciences and Biotechnology Institute (GBB), University of Groningen, Postbus 14, 9750 AA Haren, The Netherlands;Laboratory of Molecular Biology, Department of Veterinary Science, Osaka Prefecture University, 1-1 Gakuen-cho, Sakai, Osaka 599-8531, Japan

关键词: Methylotrophic yeast;    Peroxin;    Phosphoprotein;    Protein translocation;    Peroxisome biogenesis;   

DOI  :  10.1016/S0014-5793(99)01087-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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 [³²P]orthophosphate, the ³²P 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 ³²P 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.

【 授权许可】

Unknown