APOBEC-1 Complementation Factor (ACF) forms RNA-dependent multimers

作者：Galloway C A; Kumar A; Krucinska J; Smith H C^*

来源：Biochemical and Biophysical Research Communications, 2010, 398(1): 38-43.

DOI：10.1016/j.bbrc.2010.06.021

• Apolipoprotein B
• mRNA editing
• APOBEC-1
• APOBEC-1 complementation factor
• ACF
• Editosome

Limited proteolysis of APOBEC-1 complementation factor (ACF) and computational secondary structure modeling were used to guide the construction of a well-folded, truncation protein spanning residues 1-320 and containing three RNA recognition motifs (RRMs). ACF320 bound preferentially to apoB mRNA and supported APOBEC-1 dependent editing at 40% of the activity of full length ACF. Live cell FRET and immunoprecipitation assays revealed that ACF320 formed homomultimers in situ that were bridged by RNA. Our study predicted that the C to U editosome may be assembled on the mooring sequence of apoB mRNA as a dimer of ACF bound to a dimer of APOBEC-1.

• 出版日期2010-7-16