GFP-labelling of 26S proteasomes in living yeast: insight into proteasomal functions at the nuclear envelope/rough ER.
作者： Cordula Enenkel , Andrea Lehmann , Peter-Michael Kloetzel
关键词: Green fluorescent protein 、 Ubiquitin 、 Endoplasmic reticulum 、 Cell biology 、 Protein degradation 、 Protein subunit 、 Biology 、 Context (language use) 、 Proteolysis 、 Proteasome
摘要: 26S proteasomes are multisubunit protease complexes that play the central role in ubiquitin-dependent protein degradation pathway. The proteolytically active core is formed by 20S proteasome. Regulatory subunits, principally 19S cap complex, confer specificity towards ubiquitinated substrates and an ATP-dependence on proteolysis. Green fluorescence (GFP)-tagged versions of either α-subunit or ATPase subunit complex were functionally incorporated into thus allowing to monitor subcellular distribution living yeast. Our localization studies suggest proteasomal proteolysis mainly occurs at nuclear envelope (NE)/rough ER. Implications functions NE/rough ER discussed context published work with regard possible targeting mechanisms.
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