Ozimek Paulina, Kötter Peter, Veenhuis Marten, van der Klei Ida J
Eukaryotic Microbiology, Groningen Biomolecular Sciences and Biotechnology Institute, P.O. Box 14, 9750 AA Haren, The Netherlands.
FEBS Lett. 2006 Jan 9;580(1):46-50. doi: 10.1016/j.febslet.2005.11.045. Epub 2005 Dec 6.
Peroxisomal alcohol oxidase (AO) from Hansenula polymorpha is inactive and partially mislocalized to the cytosol upon synthesis in Saccharomyces cerevisiae. Co-production with H. polymorpha pyruvate carboxylase (HpPyc1p) resulted in AO activation, but did not improve import into peroxisomes. We show that import of AO mediated by S. cerevisiae Pex5p is strictly dependent on the peroxisomal targeting signal 1 (PTS1) of AO and independent of HpPyc1p. In contrast, HpPex5p-mediated sorting of AO into S. cerevisiae peroxisomes is independent of the PTS1, but requires an alternative PTS that is only formed when HpPyc1p is co-produced and most likely involves folding and co-factor binding to AO.
多形汉逊酵母的过氧化物酶体乙醇氧化酶（AO）在酿酒酵母中合成时无活性且部分错误定位于细胞质中。与多形汉逊酵母丙酮酸羧化酶（HpPyc1p）共同产生可导致AO激活，但并未改善其导入过氧化物酶体的情况。我们表明，酿酒酵母Pex5p介导的AO导入严格依赖于AO的过氧化物酶体靶向信号1（PTS1），且与HpPyc1p无关。相反，HpPex5p介导的AO分选进入酿酒酵母过氧化物酶体与PTS1无关，但需要一种仅在共同产生HpPyc1p时形成的替代PTS，并且很可能涉及AO的折叠和辅因子结合。
