1.
Biochem Biophys Res Commun
; 398(1): 38-43, 2010 Jul 16.
Article
in English
| MEDLINE
| ID: mdl-20541536
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.
Subject(s)
Heterogeneous-Nuclear Ribonucleoproteins/chemistry , Protein Multimerization , RNA/chemistry , Animals , Apolipoproteins B/genetics , Cell Line , Escherichia coli/genetics , Escherichia coli/metabolism , Heterogeneous-Nuclear Ribonucleoproteins/genetics , Humans , Protein Structure, Tertiary , RNA Editing , Rats , Recombinant Proteins/chemistry , Recombinant Proteins/genetics , Trypsin/chemistry
2.
Pol Tyg Lek
; 25(16): 577-9, 1970 Apr 20.
Article
in Polish
| MEDLINE
| ID: mdl-5422166
Subject(s)
Anemia, Hemolytic/therapy , Splenectomy , Thrombocytopenia/therapy , Adult , Female , Humans , Male , Splenomegaly/complications , Thrombocytopenia/etiology
3.
Przegl Lek
; 25(6): 490-2, 1969 Jun 24.
Article
in Polish
| MEDLINE
| ID: mdl-5805100
