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Vol 53(2019) N 4 p. 571-579; DOI 10.1134/S0026893319040071 Full Text

A.V. Morozov1*, A.V. Burov1,2, T.M. Astakhova3, D.S. Spasskaya1, B.A. Margulis4, V.L. Karpov1

Dynamics of the Functional Activity and Expression of Proteasome Subunits during Cellular Adaptation to Heat Shock

1Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, Moscow, 119991 Russia
2Faculty of Biology, Moscow State University, Moscow, 119991 Russia
3Koltsov Institute of Developmental Biology, Russian Academy of Sciences, Moscow, 119334 Russia
4Institute of Cytology, Russian Academy of Sciences, St. Petersburg, 194064 Russia

*Runkel@inbox.ru
Received - 2018-11-06; Revised - 2018-11-26; Accepted - 2018-11-26

The ubiquitin-proteasome system (UPS) performs proteolysis of most intracellular proteins. The key components of the UPS are the proteasomes, multi-subunit protein complexes, playing an important role in cellular adaptation to various types of stress. We analyzed the dynamics of the proteasome activity, the content of proteasome subunits, and the expression levels of genes encoding catalytic subunits of proteasomes in the human histiocytic lymphoma U937 cell line immediately, 2, 4, 6, 9, 24, and 48 h after a heat shock (HS). The initial decrease (up to 62%) in the proteasome activity in cellular lysates was revealed, then 10 h after HS the activity began to recover. The amount of proteasomal α-subunits in the cells decreased 2 h after HS, and was restored to 24-48 h after HS. Fluctuations in the levels of mRNAs encoding proteasome catalytic subunits with the maximum expression 2 h after HS and a gradual decrease to 48 h after HS were observed. The average estimated number of mRNA copies per cell ranged from 10 for weakly to 150 for highly expressed proteasome genes. Thus, the recovery efficiency of UPS functionality after HS, which reflects the important role of proteasomes in maintaining cell homeostasis, was evaluated.

ubiquitin-proteasome system, proteasome, heat shock



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