[Properties of endoribonuclease activity of proteasomes from K562 cells. II. Analysis of specific mRNA nucleolysis by proteasomes].
The ability of 26S proteasomes from the human proerythroleukaemic cell line K562 to degrade high-molecular-weight cytoplasmic RNAs, particularly specific messenger RNA, has been detected. The addition of hemin to K562 cells in the culture media leads to redistribution of proteasomes and their migration mainly to the cytoplasm. The human wild type p53 gene mRNA was shown to be specifically nucleolized by proteasomes. These particles displayed endoribonuclease activity towards mRNA for Renilla sp. luciferase. Proteasomes also specifically degraded Alu-containing mRNAs. A supposition is made about the involvement of proteasomes in stability control of specific RNA groups.
Mittenberg
A G
AG
Institute of Cytology RAS, St. Petersburg. agm-@mail.cytspb.rssi.ru
Kulichkova
V A
VA
Medvedeva
N D
ND
Volkova
I V
IV
Ermolaeva
Iu B
IuB
Konstantinova
I M
IM
D020087:Alu Elements; D003593:Cytoplasm / Q000378:metabolism; D004722:Endoribonucleases / Q000378:metabolism*; D016158:Genes, p53; D006427:Hemin; D006801:Humans; D020014:K562 Cells / Q000201:enzymology*; D010447:Peptide Hydrolases / Q000378:metabolism*; D046988:Proteasome Endopeptidase Complex; D012333:RNA, Messenger / Q000378:metabolism*
D012333:RNA, Messenger; D006427:Hemin; D004722:Endoribonucleases; D010447:Peptide Hydrolases; D046988:Proteasome Endopeptidase Complex; C061553:ATP dependent 26S protease