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Biochem Biophys Res Commun. 2010 Jul 16;398(1):38-43. doi: 10.1016/j.bbrc.2010.06.021. Epub 2010 Jun 10.

APOBEC-1 complementation factor (ACF) forms RNA-dependent multimers.

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1
University of Rochester, School of Medicine and Dentistry, Department of Biochemistry and Biophysics, 601 Elmwood Ave., Rochester, NY 14642, USA.

Abstract

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.

PMID:
20541536
PMCID:
PMC2912146
DOI:
10.1016/j.bbrc.2010.06.021
[Indexed for MEDLINE]
Free PMC Article
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