[Fibrillar actin promotes assembly of dissociated 20S-proteasome complex].
20S-proteasome was purified from rat liver cells by ultracentrifugation, gel-chromatography and ultrafiltration. The ability of 20S-proteasome to interact with fibrillar actin (F-actin) was examined by rapid cosidementation of these dissociated particles with F-actin in isokinetic sucrose gradient. Proteasomes, which were dissociated with Zn2+ ions, can be assembled on the fibrillar actin once again (with the exception of protein 27 kDa) at deleting ions Zn2+ from the solution with the help of EDTA.
Galkin
V E
VE
Institute of Cytology RAS, St. Petersburg.
Babakov
V N
VN
Turoverova
L V
LV
Konstantinova
I M
IM
Pinaev
G P
GP
D000199:Actins / Q000378:metabolism*; D000818:Animals; D003546:Cysteine Endopeptidases / Q000378:metabolism*; D003600:Cytosol / Q000378:metabolism; D008099:Liver / Q000378:metabolism; D008297:Male; D009097:Multienzyme Complexes / Q000378:metabolism*; D046988:Proteasome Endopeptidase Complex; D011485:Protein Binding; D051381:Rats
D000199:Actins; D009097:Multienzyme Complexes; D003546:Cysteine Endopeptidases; D046988:Proteasome Endopeptidase Complex