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

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.