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首页> 外文期刊>Molecular and Cellular Biology >Activation of a Novel Ubiquitin-Independent Proteasome Pathway when RNA Polymerase II Encounters a Protein Roadblock
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Activation of a Novel Ubiquitin-Independent Proteasome Pathway when RNA Polymerase II Encounters a Protein Roadblock

机译：RNA聚合酶II遇到蛋白质路障时，新型的泛素依赖性蛋白酶体途径的激活。

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Topoisomerase IIβ (Top2β)-DNA cleavage complexes are known to arrest elongating RNA polymerase II (RNAPII), triggering a proteasomal degradation of the RNAPII large subunit (RNAPII LS) and Top2β itself as a prelude to DNA repair. Here, we demonstrate that the degradation of Top2β occurs through a novel ubiquitin-independent mechanism that requires only 19S AAA ATPases and 20S proteasome. Our results suggest that 19S AAA ATPases play a dual role in sensing the Top2β cleavage complex and coordinating its degradation by 20S proteasome when RNAPII is persistently stalled by the Top2β protein roadblock. Clarification of this transcription-associated proteasome pathway could shed light on a general role of 19S AAA ATPases in processing tight protein-DNA complexes during transcription elongation.
机译：已知拓扑异构酶IIβ（Top2β）-DNA切割复合物会阻止延长的RNA聚合酶II（RNAPII），从而触发RNAPII大亚基（RNAPII LS）和Top2β本身的蛋白酶体降解，作为DNA修复的序幕。在这里，我们证明了Top2β的降解是通过一种新型的，与泛素无关的机制发生的，该机制仅需要19S AAA ATPase和20S蛋白酶体。我们的结果表明，当RNAPII被Top2β蛋白质阻滞剂持续阻滞时，19S AAA ATPases在感知Top2β裂解复合物和协调其被20S蛋白酶体降解中起双重作用。此转录相关的蛋白酶体途径的澄清可能阐明19S AAA ATPases在转录延伸过程中处理紧密的蛋白质DNA复合物的一般作用。

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