Nucleocytoplasmic trafficking of the molecular chaperone Hsp104 in unstressed and heat-shocked cells.
作者： Johnny M. Tkach , John R. Glover
DOI: 10.1111/J.1600-0854.2007.00666.X
关键词:
摘要: Hsp104 is a molecular chaperone in yeast that restores solubility and activity to inactivated proteins after severe heat shock. We investigated the mechanisms influence subcellular distribution both unstressed heat-shocked cells. In cells, green fluorescent protein-Hsp104 fusion protein were detected nucleus cytoplasm. demonstrate 17-amino-acid sequence of nuclear localization 17 (NLS17) sufficient target reporter molecule also necessary for normal distribution. The targeting function NLS17 genetically dependent on KAP95 KAP121. addition, wild-type Hsp104, but not an NLS17-mutated variant, accumulated cells depleted general export factor Xpo1. Interestingly, severe, nonlethal shock enhances levels NLS17-independent manner. Under these conditions, we karyopherin-mediated transport impaired, while integrity nuclear-cytoplasmic barrier remains intact. Based observations, propose continues access during using karyopherin-independent mechanism.
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