Native structure of rat liver immune proteasomes


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Native structure of active forms of rat liver immune proteasomes has been studied by two-dimensional electrophoresis method modified for analysis of unpurified protein fractions. The developed method allowed revealing the proteasome immune subunits LMP7 and LMP2 in 20S subparticles and in the structures bound to one or two PA28αβ activators, but not to the PA700 activator, which is involved in the hydrolysis of ubiquitinated proteins. The results obtained indicate the participation of the immune proteasomes in delicate regulatory mechanisms based on the production of biologically active peptides and exclude their participation in processes of crude degradation of “rotated” ubiquitinated proteins.

作者简介

A. Stepanova

Koltzov Institute of Developmental Biology

Email: npsharova@bk.ru
俄罗斯联邦, ul. Vavilova 26, Moscow, 119334

Yu. Lyupina

Koltzov Institute of Developmental Biology

Email: npsharova@bk.ru
俄罗斯联邦, ul. Vavilova 26, Moscow, 119334

N. Sharova

Koltzov Institute of Developmental Biology

编辑信件的主要联系方式.
Email: npsharova@bk.ru
俄罗斯联邦, ul. Vavilova 26, Moscow, 119334

P. Erokhov

Koltzov Institute of Developmental Biology

Email: npsharova@bk.ru
俄罗斯联邦, ul. Vavilova 26, Moscow, 119334

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