[Novel endoribonuclease activity of 26S-proteasomes from A-431 cells].
Our analysis detected in 26S proteasomes of human A-431 cells a strong endoribonuclease activity, degrading cytoplasmic high-molecular-mass RNA, particularly, specific mRNAs. Enzymatic nature of this activity has been confirmed, and the optimal conditions studied. This endonuclease activity of proteasomes has not been earlier observed. Proteasome involvement in the stability control of specific messenger RNA molecules is suggested, and proteasome participation in the coordinated control of various stages of gene expression is discussed.
Evteeva
I N
IN
Institute of Cytology RAS, St. Petersburg.
Kulichkova
V A
VA
Mittenberg
A G
AG
Volkova
I V
IV
Ermolaeva
Iu B
IuB
Teslenko
L V
LV
Obukhova
A D
AD
Penniiaĭnen
V A
VA
Gauze
L N
LN
Konstantinova
I M
IM
D004722:Endoribonucleases / Q000378:metabolism*; D006801:Humans; D010447:Peptide Hydrolases / Q000378:metabolism*; D046988:Proteasome Endopeptidase Complex; D014407:Tumor Cells, Cultured
D004722:Endoribonucleases; D010447:Peptide Hydrolases; D046988:Proteasome Endopeptidase Complex; C061553:ATP dependent 26S protease