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Literature DB >> 20541536

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

C A Galloway¹, A Kumar, J Krucinska, H C Smith.

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. Copyright 2010 Elsevier Inc. All rights reserved.

Entities: CellLine Chemical Disease Gene Species

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Year: 2010 PMID： 20541536 PMCID： PMC2912146 DOI： 10.1016/j.bbrc.2010.06.021

Source DB: PubMed Journal: Biochem Biophys Res Commun ISSN： 0006-291X Impact factor: 3.575

35 in total

1. A method for directly fitting the time derivative of sedimentation velocity data and an alternative algorithm for calculating sedimentation coefficient distribution functions.

Authors: J S Philo
Journal: Anal Biochem Date: 2000-03-15 Impact factor: 3.365

2. The NMR structure of the 38 kDa U1A protein - PIE RNA complex reveals the basis of cooperativity in regulation of polyadenylation by human U1A protein.

Authors: L Varani; S I Gunderson; I W Mattaj; L E Kay; D Neuhaus; G Varani
Journal: Nat Struct Biol Date: 2000-04

3. Measuring editing activity and identifying cytidine-to-uridine mRNA editing factors in cells and biochemical isolates.

Authors: Harold C Smith
Journal: Methods Enzymol Date: 2007 Impact factor: 1.600

4. Isolation, characterization and developmental regulation of the human apobec-1 complementation factor (ACF) gene.

Authors: J O Henderson; V Blanc; N O Davidson
Journal: Biochim Biophys Acta Date: 2001-11-11

5. Identification of the yeast cytidine deaminase CDD1 as an orphan C-->U RNA editase.

Authors: G S Dance; P Beemiller; Y Yang; D V Mater; I S Mian; H C Smith
Journal: Nucleic Acids Res Date: 2001-04-15 Impact factor: 16.971

6. Mutagenesis of apobec-1 complementation factor reveals distinct domains that modulate RNA binding, protein-protein interaction with apobec-1, and complementation of C to U RNA-editing activity.

Authors: V Blanc; J O Henderson; S Kennedy; N O Davidson
Journal: J Biol Chem Date: 2001-09-24 Impact factor: 5.157

7. Molecular cloning of apobec-1 complementation factor, a novel RNA-binding protein involved in the editing of apolipoprotein B mRNA.

Authors: A Mehta; M T Kinter; N E Sherman; D M Driscoll
Journal: Mol Cell Biol Date: 2000-03 Impact factor: 4.272

8. Purification and molecular cloning of a novel essential component of the apolipoprotein B mRNA editing enzyme-complex.

Authors: H Lellek; R Kirsten; I Diehl; F Apostel; F Buck; J Greeve
Journal: J Biol Chem Date: 2000-06-30 Impact factor: 5.157

9. Structural basis for recognition of AU-rich element RNA by the HuD protein.

Authors: X Wang; T M Tanaka Hall
Journal: Nat Struct Biol Date: 2001-02

10. The editosome for cytidine to uridine mRNA editing has a native complexity of 27S: identification of intracellular domains containing active and inactive editing factors.

Authors: Mark P Sowden; Nazzareno Ballatori; Karen L de Mesy Jensen; Lakesha Hamilton Reed; Harold C Smith
Journal: J Cell Sci Date: 2002-03-01 Impact factor: 5.285

7 in total

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

1. A method for directly fitting the time derivative of sedimentation velocity data and an alternative algorithm for calculating sedimentation coefficient distribution functions.

2. The NMR structure of the 38 kDa U1A protein - PIE RNA complex reveals the basis of cooperativity in regulation of polyadenylation by human U1A protein.

3. Measuring editing activity and identifying cytidine-to-uridine mRNA editing factors in cells and biochemical isolates.

4. Isolation, characterization and developmental regulation of the human apobec-1 complementation factor (ACF) gene.

5. Identification of the yeast cytidine deaminase CDD1 as an orphan C-->U RNA editase.

6. Mutagenesis of apobec-1 complementation factor reveals distinct domains that modulate RNA binding, protein-protein interaction with apobec-1, and complementation of C to U RNA-editing activity.

7. Molecular cloning of apobec-1 complementation factor, a novel RNA-binding protein involved in the editing of apolipoprotein B mRNA.

8. Purification and molecular cloning of a novel essential component of the apolipoprotein B mRNA editing enzyme-complex.

9. Structural basis for recognition of AU-rich element RNA by the HuD protein.

10. The editosome for cytidine to uridine mRNA editing has a native complexity of 27S: identification of intracellular domains containing active and inactive editing factors.

Review 1. Functions and regulation of the APOBEC family of proteins.

Review 2. Role of the gut in lipid homeostasis.

3. Identification of DNA cleavage- and recombination-specific hnRNP cofactors for activation-induced cytidine deaminase.

4. Comparison of RNA Editing Activity of APOBEC1-A1CF and APOBEC1-RBM47 Complexes Reconstituted in HEK293T Cells.

5. Structural and functional assessment of APOBEC3G macromolecular complexes.

Review 6. The APOBEC Protein Family: United by Structure, Divergent in Function.

7. Flow-cytometric visualization of C>U mRNA editing reveals the dynamics of the process in live cells.