A cytosolic factor binds to the c-myc A + U-rich element and specifically destabilizes c-myc mRNA in a cell-free system, with RNA binding and degradation appearing to be separable functions.
This basic science study identifies a cytosolic factor that regulates c-myc mRNA stability, demonstrating that RNA substrate binding and degradation are separable functions.
Transient expression of some proto-oncogenes, cytokines, and transcription factors occurs as a cellular response to growth factors, 12-O-tetradecanoylphorbol-13-acetate, antigen stimulation, or inflammation. Expression of these genes is mediated in part by the rapid turnover of their mRNAs. A + U-rich elements in the 3' untranslated regions of these mRNAs serve as one recognition signal targeting the mRNAs for rapid degradation. I report the identification of a cytosolic factor that both binds to the proto-oncogene c-myc A + U-rich element and specifically destabilizes c-myc mRNA in a cell-free mRNA decay system which reconstitutes mRNA decay processes found in cells. Proteinase K treatment of the factor abolishes its c-myc mRNA degradation activity without affecting its RNA-binding capacity. Thus, RNA substrate binding and degradation appear to be separable functions. These findings should aid in understanding how the cell selectively targets mRNAs for rapid turnover.
Gary Brewer (Wed,) reported a other. Cytosolic RNA-binding factor was evaluated on c-myc mRNA stability and degradation. A cytosolic factor binds to the c-myc A + U-rich element and specifically destabilizes c-myc mRNA in a cell-free system, with RNA binding and degradation appearing to be separable functions.