Comparative analysis of proteins associated with 26S and 20S proteasomes isolated from rabbit brain and liver

Buneeva O.A.1 , Kopylov A.T.1, Zgoda V.G.1, Gnedenko O.V.1, Kaloshina S.A.1, Medvedeva M.V.2, Ivanov A.S.1, Medvedev A.E.1

1. Institute of Biomedical Chemistry, Moscow, Russia
2. Lomonosov Moscow State University, Biological Faculty, Moscow, Russia
Section: Experimental Study
DOI: 10.18097/PBMC20226801018      PubMed Id: 35221293
Year: 2022  Volume: 68  Issue: 1  Pages: 18-31
We have isolated fractions of 26S and 20S proteasomes were from the rabbit liver and the brain. According to mass spectrometric (MS) analysis, the 26S proteasome fractions from these organs contained catalytic and regulatory subunits characteristic of the proteasome core and regulatory subunits. The 20S fractions of brain and liver proteasomes contained only catalytic proteasome subunits. In addition to proteasome subunits, the isolated fractions contained components of the ubiquitin-proteasome system, ubiquitinated proteins, enzymes that play an important role in metabolic processes, cytoskeletal components, signaling, regulatory, and protective proteins, as well as proteins regulating gene expression, cell division, and differentiation. The abundance of a number of proteasome-associated proteins was comparable or exceeded the abundance of intrinsic proteasome components. About a third of the proteins common to all studied fractions (26S and 20S of brain and liver proteasomes) belong to the group of multifunctional proteins. Selective biosensor validation confirmed the affinity binding of proteins (aldolase, phosphoglycerate kinase) identified during MS analysis to the brain 20S proteasome. Comparison of the subproteomes of the 26S and 20S brain proteasomes showed that removal of components of the regulatory (19S) subparticles caused almost two-fold increase in the total number of individual proteins associated with the core part of the proteasome (20S). In the liver, the number of proteins associated with the core part of the proteasome remained basically unchanged after the removal of the components of the regulatory (19S) subparticles. This indicates that in the brain and, possibly, in other organs, proteins of the regulatory (19S) subunit play an important role in the formation of the proteasome interactome.
Download PDF:  
Keywords: 26S and 20S proteasomes, ubiquitin-proteasome system, subproteome, biosensor, moonlighting proteins
Supplementary materials:

Buneeva, O. A., Kopylov, A. T., Zgoda, V. G., Gnedenko, O. V., Kaloshina, S. A., Medvedeva, M. V., Ivanov, A. S., Medvedev, A. E. (2022). Comparative analysis of proteins associated with 26S and 20S proteasomes isolated from rabbit brain and liver. Biomeditsinskaya Khimiya, 68(1), 18-31.
This paper is also available as the English translation: 10.1134/S1990750822030040
 2023 (vol 69)
 2022 (vol 68)
 2021 (vol 67)
 2020 (vol 66)
 2019 (vol 65)
 2018 (vol 64)
 2017 (vol 63)
 2016 (vol 62)
 2015 (vol 61)
 2014 (vol 60)
 2013 (vol 59)
 2012 (vol 58)
 2011 (vol 57)
 2010 (vol 56)
 2009 (vol 55)
 2008 (vol 54)
 2007 (vol 53)
 2006 (vol 52)
 2005 (vol 51)
 2004 (vol 50)
 2003 (vol 49)