Inactivation of theHansenula polymorpha PMR1gene affects cell viability and functioning of the secretory pathway

• DOI: 10.1111/j.1567-1364.2007.00247.x
• Publication Date: 2007-05-10T10:43:09Z
• Authors: M.O. Agaphonov; T.A. Plotnikova; A.V. Fokina; N.V. Romanova; A.N. Packeiser; H.A. Kang; M.D. Ter-Avanesyan
• Keywords: Secretory protein

In yeast, functions of the endoplasmic reticulum (ER) depend on Golgi apparatus Ca2+ pool, which is replenished by medial-Golgi ion pump Pmr1p. Here, to dissect role pool in protein folding and elimination unfolded proteins ER, manifestations pmr1 mutation yeast Hansenula polymorpha were studied. The PMR1 gene was disrupted a H. diploid strain. Haploid segregants this bearing disruption allele viable, though they showed severe growth defect synthetic medium rapidly died during storage at low temperature. Disruption led defects Golgi-hosted glycosylation vacuolar sorting. This increased survival rate cells upon treatment with proapoptotic drug amiodarone. Unlike Saccharomyces cerevisiae, mutant not hypersensitive chemicals that induce accumulation indicating from ER essentially affected. At same time, improved secretion human urokinase decreased its intracellular aggregation, an influence ER.