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蛋白酶体复合物对真核转录激活的多种调控机制。

Diverse regulatory mechanisms of eukaryotic transcriptional activation by the proteasome complex.

作者信息

Bhaumik Sukesh R, Malik Shivani

机构信息

Department of Biochemistry and Molecular Biology, Southern Illinois University School of Medicine, Carbondale, IL 62901, USA.

出版信息

Crit Rev Biochem Mol Biol. 2008 Nov-Dec;43(6):419-33. doi: 10.1080/10409230802605914.

DOI:10.1080/10409230802605914
PMID:19058045
Abstract

The life of any protein within a cell begins with transcriptional activation, and ends with proteolytic degradation. Intriguingly, the 26S proteasome complex, a non-lysosomal protein degradation machine comprising the 20S proteolytic core and 19S regulatory particles, has been implicated in intimate regulation of eukaryotic transcriptional activation through diverse mechanisms in a proteolysis-dependent as well as independent manner. Here, we discuss the intricate mechanisms of such proteasomal regulation of eukaryotic gene activation via multiple pathways.

摘要

细胞内任何蛋白质的生命始于转录激活,终于蛋白水解降解。有趣的是,26S蛋白酶体复合物是一种非溶酶体蛋白降解机器,由20S蛋白水解核心和19S调节颗粒组成,已被证明通过多种机制以蛋白水解依赖和独立的方式密切调节真核转录激活。在这里,我们讨论通过多种途径对真核基因激活进行这种蛋白酶体调节的复杂机制。

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