ПОЛУЧЕНИЕ С-КОНЦЕВОГО УЧАСТКА БЕЛКА PI31 ДЛЯ ИНГИБИРОВАНИЯ АКТИВНОСТИ 20S-ПРОТЕАСОМЫ IN VITRO.

Е.Е. Дьяконов, Е.А. Малкина, В.А. Куличкова, А.Н. Томилин, А.С. Цимоха

Research output: Contribution to journalArticle

Abstract

The proteasome inhibitor PI31 protein is 271 amino acid residues long and contains N-terminal globular domain and C-terminal proline-rich domain. The proteasome inhibition is conferred by the C-terminal proline-rich domain of PI31. E. coli recombinant expression construct of a fusion protein 6His-cPI31 consisting of C-terminal domain of PI31 (151–271 a. a.) and the N-terminal His-tag was made. The expressed protein was purified using nickel-agarose affinity chromatography. The recombinant protein 6His-cPI31 inhibited chymotrypsin-like activity of 20S proteasome, but not 26S-proteasome in vitro.
Original languageRussian
Pages (from-to)301-307
JournalЦитология
Volume61
Issue number4
StatePublished - 2019
Externally publishedYes

Keywords

  • proteasome
  • Proteasome inhibitor PI31
  • proteolysis
  • ингибитор протеасомы PI31
  • протеасома
  • протеолиз

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