We have shown previously that the decay of human bcl-2 mRNA is mediated by an adenine/uridine-rich element (ARE) located in the 3′-untranslated region. Here, we have utilized a non-radioactive cell-free mRNA decay system to investigate the biochemical and functional mechanisms regulating the ARE-dependent degradation of bcl-2 mRNA. Using RNA substrates, mutants, and competitors, we found that decay is specific and ARE-dependent, although maximized by the ARE-flanking regions. In unfractionated extracts from different cell types and in whole cells, the relative enzymatic activity was related to the amount of Bcl-2 protein expressed by the cells at steady state. The degradation activity was lost upon Bcl-2 depletion and was reconstituted by adding recombinant Bcl-2. Ineffective extracts from cells that constitutively do not express Bcl-2 acquire full degradation activity by adding recombinant Bcl-2 protein. We conclude that Bcl-2 is necessary to activate the degradation complex on the relevant RNA target.
Bcl-2 protein is required for the adenine/uridine-rich element (ARE)-dependent degradation of its own messenger / A. Bevilacqua, M.C. Ceriani, G. Canti, L. Asnaghi, R. Gherzi, G. Brewer, L. Papucci, N. Schiavone, S. Capaccioli, A. Nicolin. - In: THE JOURNAL OF BIOLOGICAL CHEMISTRY. - ISSN 0021-9258. - 278:26(2003), pp. 23451-23459.
|Titolo:||Bcl-2 protein is required for the adenine/uridine-rich element (ARE)-dependent degradation of its own messenger|
BEVILACQUA, ANNAMARIA (Primo)
NICOLIN, ANGELO NICOLO' (Ultimo)
|Settore Scientifico Disciplinare:||Settore BIO/14 - Farmacologia|
|Data di pubblicazione:||2003|
|Digital Object Identifier (DOI):||http://dx.doi.org/10.1074/jbc.M210620200|
|Appare nelle tipologie:||01 - Articolo su periodico|