Open AccessA human RNase E-like activity that cleaves RNA sequences involved in mRNA stability control.
Author(s) -
Anders Wennborg,
Björn Sohlberg,
Doris Angerer,
Gracjana Klein,
Alexander von Gabain
Publication year - 1995
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.92.16.7322
Subject(s) - rnase p , rna , rnase h , biology , messenger rna , microbiology and biotechnology , rnase mrp , degradosome , nuclease protection assay , untranslated region , ribonuclease iii , escherichia coli , non coding rna , rnase ph , biochemistry , gene , rna interference
We have detected an endoribonucleolytic activity in human cell extracts that processes the Escherichia coli 9S RNA and outer membrane protein A (ompA) mRNA with the same specificity as RNase E from E. coli. The human enzyme was partially purified by ion-exchange chromatography, and the active fractions contained a protein that was detected with antibodies shown to recognize E. coli RNase E. RNA containing four repeats of the destabilizing motif AUUUA and RNA from the 3' untranslated region of human c-myc mRNA were also found to be cleaved by E. coli RNase E and its human counterpart in a fashion that may suggest a role of this activity in mammalian mRNA decay. It was also found that RNA containing more than one AUUUA motif was cleaved more efficiently than RNA with only one or a mutated motif. This finding of a eukaryotic endoribonucleolytic activity corresponding to RNase E indicates an evolutionary conservation of the components of mRNA degradation systems.