ArticleRNA (New York, N.Y.)2002
Identification of domains in apobec-1 complementation factor required for RNA binding and apolipoprotein-B mRNA editing.
Article in RNA (New York, N.Y.), 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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Who cites it
37 citing papers in PubMed.
- Deciphering APOBEC1 in Avians: unravelling loss events and functional insights.Immunogenetics · 2026Article
- An evolutionarily conserved tryptophan cage promotes folding of the extended RNA recognition motif in the hnRNPR-like protein family.Protein science : a publication of the Protein Society · 2025Article
- Identification of RBM46 as a novel APOBEC1 cofactor for C-to-U RNA-editing activity.Journal of molecular biology · 2023Article
- C-to-U RNA deamination is the driving force accelerating SARS-CoV-2 evolution.Life science alliance · 2023Article
- RNA binding motif 47 (RBM47): emerging roles in vertebrate development, RNA editing and cancer.Molecular and cellular biochemistry · 2021Review
- Review
- RNA Editing and Its Roles in Plant Organelles.Frontiers in genetics · 2021Review
- Comparison of RNA Editing Activity of APOBEC1-A1CF and APOBEC1-RBM47 Complexes Reconstituted in HEK293T Cells.Journal of molecular biology · 2019Article
- Apobec1 complementation factor (A1CF) and RBM47 interact in tissue-specific regulation of C to U RNA editing in mouse intestine and liver.RNA (New York, N.Y.) · 2019Article
- Review
- Identification of Receptor Ligands in Apo B100 Reveals Potential Functional Domains.The protein journal · 2018Article
- A rice dual-localized pentatricopeptide repeat protein is involved in organellar RNA editing together with OsMORFs.Journal of experimental botany · 2018Article
- The landscape of miRNA editing in animals and its impact on miRNA biogenesis and targeting.Genome research · 2018Article
- Epitranscriptomic profiling across cell types reveals associations between APOBEC1-mediated RNA editing, gene expression outcomes, and cellular function.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Review
- APOBEC1 complementation factor (A1CF) is dispensable for C-to-U RNA editing in vivo.RNA (New York, N.Y.) · 2017Article
- EIYMNVPV Motif is Essential for A1CF Nucleus Localization and A1CF (-8aa) Promotes Proliferation of MDA-MB-231 Cells via Up-Regulation of IL-6.International journal of molecular sciences · 2016Article
- Apobec-1 Complementation Factor (A1CF) Inhibits Epithelial-Mesenchymal Transition and Migration of Normal Rat Kidney Proximal Tubular Epithelial Cells.International journal of molecular sciences · 2016Article
- RNA Editing-Systemic Relevance and Clue to Disease Mechanisms?Frontiers in molecular neuroscience · 2016Review
- Identification of DNA cleavage- and recombination-specific hnRNP cofactors for activation-induced cytidine deaminase.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
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Authors and funding
2 authors.
Funding
Abstract
The C-to-U editing of apolipoprotein-B (apo-B) mRNA is catalyzed by an enzyme complex that recognizes an 11-nt mooring sequence downstream of the editing site. A minimal holoenzyme that edits apo-B mRNA in vitro has been defined. This complex contains apobec-1, the catalytic subunit, and apobec-1 complementation factor (ACF), the RNA-binding subunit that binds to the mooring sequence. Here, we show that ACF binds with high affinity to single-stranded but not double-stranded apo-B mRNA. ACF contains three nonidentical RNA recognition motifs (RRM) and a unique C-terminal auxiliary domain. In many multi-RRM proteins, the RRMs mediate RNA binding and an auxiliary domain functions in protein-protein interactions. Here we show that ACF does not fit this simple model. Based on deletion mutagenesis, the RRMs in ACF are necessary but not sufficient for binding to apo-B mRNA. Amino acids in the pre-RRM region are required for complementing activity and RNA binding, but not for interaction with apobec-1. The C-terminal 196 amino acids are not absolutely essential for function. However, further deletion of an RG-rich region from the auxiliary domain abolished complementing activity, RNA binding, and apobec-1 interaction. The auxiliary domain alone did not bind apobec-1. Although all three RRMs are required for complementing activity and apobec-1 interaction, the individual motifs contribute differently to RNA binding. Point mutations in RRM1 or RRM2 decreased the Kd for apo-B mRNA by two orders of magnitude whereas mutations in RRM3 reduced binding affinity 13-fold. The pairwise expression of RRM1 with RRM2 or RRM3 resulted in moderate affinity binding.
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