APOBEC-1 complementation factor (ACF) forms RNA-dependent multimers.
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.
Galloway
C A
CA
University of Rochester, School of Medicine and Dentistry, Department of Biochemistry and Biophysics, 601 Elmwood Ave., Rochester, NY 14642, USA.
Kumar
A
A
Krucinska
J
J
Smith
H C
HC
D000818:Animals; D001055:Apolipoproteins B / Q000235:genetics; D002460:Cell Line; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism; D034441:Heterogeneous-Nuclear Ribonucleoproteins / Q000737:chemistry* / Q000235:genetics; D006801:Humans; D055503:Protein Multimerization; D017434:Protein Structure, Tertiary; D012313:RNA / Q000737:chemistry*; D017393:RNA Editing; D051381:Rats; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics; D014357:Trypsin / Q000737:chemistry
C511990:APOBEC-1 complementation factor, rat; D001055:Apolipoproteins B; D034441:Heterogeneous-Nuclear Ribonucleoproteins; D011994:Recombinant Proteins; D012313:RNA; D014357:Trypsin