Regulation of Endoribonuclease Activity of Alpha-Type Proteasome Subunits in Proerythroleukemia K562 Upon Hemin-Induced Differentiation

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• 作者：Alexey G. Mittenberg ; Tatyana N. Moiseeva ; Valeria O. Kuzyk…
• 关键词：Proteasome ; Endoribonuclease activity ; Posttranslational modifications ; Phosphorylation ; Ubiquitylation ; Differentiation
• 刊名：The Protein Journal
• 出版年：2016
• 出版时间：February 2016
• 年：2016
• 卷：35
• 期：1
• 页码：17-23
• 全文大小：2,439 KB
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• 作者单位：Alexey G. Mittenberg (1)
  Tatyana N. Moiseeva (1)
  Valeria O. Kuzyk (1)
  Nickolai A. Barlev (1)
  
  1. Institute of Cytology of the Russian Academy of Sciences, St. Petersburg, Russia, 194064
  
• 刊物类别：Chemistry and Materials Science
• 刊物主题：Chemistry
  Bioorganic Chemistry
  Biochemistry
  Organic Chemistry
  Animal Anatomy, Morphology and Histology
  
• 出版者：Springer Netherlands
• ISSN：1573-4943

文摘

The proteasome is the main intracellular proteolytic machine involved in the regulation of numerous cellular processes, including gene expression. In addition to their proteolytic activity, proteasomes also exhibit ATPase/helicase (the 19S particle) and RNAse (the 20S particle) activities, which are regulated by post-translational modifications. In this report we uncovered that several 20S particle subunits: α1 (PSMA6), α2 (PSMA2), α4 (PSMA7), α5 (PSMA5), α6 (PSMA1) and α7 (PSMA3) possess RNAse activity against the p53 mRNA in vitro. Furthermore, we found that the RNAse activity of PSMA1 and PSMA3 was regulated upon hemin-induced differentiation of K562 proerythroleukemia cells. The decrease in RNAse activity of PSMA1 and PSMA3 was paralleled by changes in their status of phosphorylation and ubiquitylation. Collectively, our data support the notion that proteasomal RNAse activity may be functionally important and provide insights into the potential mechanism of p53 repression in erythroleukemia cells by RNAse activity of the 20S α-type subunits. Keywords Proteasome Endoribonuclease activity Posttranslational modifications Phosphorylation Ubiquitylation Differentiation