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 prote...

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Bibliographic Details
Published inT͡S︡itologii͡a Vol. 42; no. 7; p. 675
Main Authors Evteeva, I N, Kulichkova, V A, Mittenberg, A G, Volkova, I V, Ermolaeva, Iu B, Teslenko, L V, Obukhova, A D, Penniiaĭnen, V A, Gauze, L N, Konstantinova, I M
Format Journal Article
LanguageRussian
Published Russia (Federation) 2000
Subjects
Endoribonucleases - metabolism
Humans
Peptide Hydrolases - metabolism
Proteasome Endopeptidase Complex
Tumor Cells, Cultured
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Summary: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.
ISSN:0041-3771