作者: Diana A. Stavreva , Miyuki Kawasaki , Miroslav Dundr , Karel Koberna , Waltraud G. Müller
DOI: 10.1128/MCB.02227-05
关键词:
摘要: We have investigated the possible involvement of ubiquitin-proteasome system (UPS) in ribosome biogenesis. find by immunofluorescence that ubiquitin is present within nucleoli and also demonstrate immunoprecipitation complexes associated with pre-rRNA processing factors are ubiquitinated. Using short proteasome inhibition treatments, we show fluorescence microscopy nucleolar morphology disrupted for some but not all involved Interference degradation induces accumulation 90S preribosomes, alters dynamic properties a number factors, slows release mature rRNA from nucleolus, leads to depletion 18S 28S rRNAs. Together, these results suggest UPS probably at many steps during biogenesis, including maturation preribosome.