C to U RNA editing mediated by APOBEC1 requires RNA-binding protein RBM47

Nicolas Fossat*, Karin Tourle, Tania Radziewic, Kristen Barratt, Doreen Liebhold, Joshua B. Studdert, Melinda Power, Vanessa Jones, David A.F. Loebel, Patrick P.L. Tam

*Corresponding author for this work

Research output: Contribution to journalArticleResearchpeer-review

43 Citations (Scopus)

Abstract

Cytidine (C) to Uridine (U) RNA editing is a post-transcriptional modification that is accomplished by the deaminase APOBEC1 and its partnership with the RNA-binding protein A1CF. We identify and characterise here a novel RNA-binding protein, RBM47, that interacts with APOBEC1 and A1CF and is expressed in tissues where C to U RNA editing occurs. RBM47 can substitute for A1CF and is necessary and sufficient for APOBEC1-mediated editing in vitro. Editing is further impaired in Rbm47-deficient mutant mice. These findings suggest that RBM47 and APOBEC1 constitute the basic machinery for C to U RNA editing. Synopsis The RNA-binding protein RBM47 is required for normal Cytidine to Uridine RNA editing in mice and is sufficient for the C to U editing activity of APOBEC1, indicating that the composition of the editosome holoenzyme needs to be revised. RBM47 is found in the epithelial cells of the intestine and interacts with APOBEC1 and A1CF. RBM47 can replace A1CF and is sufficient with APOBEC1 for C to U RNA editing. C to U editing of Apob and other RNA is impaired in Rbm47-deficient mice. The RNA-binding protein RBM47 is required for normal Cytidine to Uridine RNA editing in mice and is sufficient for the C to U editing activity of APOBEC1, indicating that the composition of the editosome holoenzyme needs to be revised.

Original languageEnglish
Pages (from-to)903-910
Number of pages8
JournalEMBO Reports
Volume15
Issue number8
DOIs
Publication statusPublished - 2014
Externally publishedYes

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RNA Editing
RNA-Binding Proteins
RNA
Cytidine
Uridine
Holoenzymes
Apolipoproteins B
Intestines
Chemical analysis
Machinery
Epithelial Cells
Tissue

Cite this

Fossat, N., Tourle, K., Radziewic, T., Barratt, K., Liebhold, D., Studdert, J. B., ... Tam, P. P. L. (2014). C to U RNA editing mediated by APOBEC1 requires RNA-binding protein RBM47. EMBO Reports, 15(8), 903-910. https://doi.org/10.15252/embr.201438450
Fossat, Nicolas ; Tourle, Karin ; Radziewic, Tania ; Barratt, Kristen ; Liebhold, Doreen ; Studdert, Joshua B. ; Power, Melinda ; Jones, Vanessa ; Loebel, David A.F. ; Tam, Patrick P.L. / C to U RNA editing mediated by APOBEC1 requires RNA-binding protein RBM47. In: EMBO Reports. 2014 ; Vol. 15, No. 8. pp. 903-910.
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title = "C to U RNA editing mediated by APOBEC1 requires RNA-binding protein RBM47",
abstract = "Cytidine (C) to Uridine (U) RNA editing is a post-transcriptional modification that is accomplished by the deaminase APOBEC1 and its partnership with the RNA-binding protein A1CF. We identify and characterise here a novel RNA-binding protein, RBM47, that interacts with APOBEC1 and A1CF and is expressed in tissues where C to U RNA editing occurs. RBM47 can substitute for A1CF and is necessary and sufficient for APOBEC1-mediated editing in vitro. Editing is further impaired in Rbm47-deficient mutant mice. These findings suggest that RBM47 and APOBEC1 constitute the basic machinery for C to U RNA editing. Synopsis The RNA-binding protein RBM47 is required for normal Cytidine to Uridine RNA editing in mice and is sufficient for the C to U editing activity of APOBEC1, indicating that the composition of the editosome holoenzyme needs to be revised. RBM47 is found in the epithelial cells of the intestine and interacts with APOBEC1 and A1CF. RBM47 can replace A1CF and is sufficient with APOBEC1 for C to U RNA editing. C to U editing of Apob and other RNA is impaired in Rbm47-deficient mice. The RNA-binding protein RBM47 is required for normal Cytidine to Uridine RNA editing in mice and is sufficient for the C to U editing activity of APOBEC1, indicating that the composition of the editosome holoenzyme needs to be revised.",
author = "Nicolas Fossat and Karin Tourle and Tania Radziewic and Kristen Barratt and Doreen Liebhold and Studdert, {Joshua B.} and Melinda Power and Vanessa Jones and Loebel, {David A.F.} and Tam, {Patrick P.L.}",
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Fossat, N, Tourle, K, Radziewic, T, Barratt, K, Liebhold, D, Studdert, JB, Power, M, Jones, V, Loebel, DAF & Tam, PPL 2014, 'C to U RNA editing mediated by APOBEC1 requires RNA-binding protein RBM47', EMBO Reports, vol. 15, no. 8, pp. 903-910. https://doi.org/10.15252/embr.201438450

C to U RNA editing mediated by APOBEC1 requires RNA-binding protein RBM47. / Fossat, Nicolas; Tourle, Karin; Radziewic, Tania; Barratt, Kristen; Liebhold, Doreen; Studdert, Joshua B.; Power, Melinda; Jones, Vanessa; Loebel, David A.F.; Tam, Patrick P.L.

In: EMBO Reports, Vol. 15, No. 8, 2014, p. 903-910.

Research output: Contribution to journalArticleResearchpeer-review

TY - JOUR

T1 - C to U RNA editing mediated by APOBEC1 requires RNA-binding protein RBM47

AU - Fossat, Nicolas

AU - Tourle, Karin

AU - Radziewic, Tania

AU - Barratt, Kristen

AU - Liebhold, Doreen

AU - Studdert, Joshua B.

AU - Power, Melinda

AU - Jones, Vanessa

AU - Loebel, David A.F.

AU - Tam, Patrick P.L.

PY - 2014

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N2 - Cytidine (C) to Uridine (U) RNA editing is a post-transcriptional modification that is accomplished by the deaminase APOBEC1 and its partnership with the RNA-binding protein A1CF. We identify and characterise here a novel RNA-binding protein, RBM47, that interacts with APOBEC1 and A1CF and is expressed in tissues where C to U RNA editing occurs. RBM47 can substitute for A1CF and is necessary and sufficient for APOBEC1-mediated editing in vitro. Editing is further impaired in Rbm47-deficient mutant mice. These findings suggest that RBM47 and APOBEC1 constitute the basic machinery for C to U RNA editing. Synopsis The RNA-binding protein RBM47 is required for normal Cytidine to Uridine RNA editing in mice and is sufficient for the C to U editing activity of APOBEC1, indicating that the composition of the editosome holoenzyme needs to be revised. RBM47 is found in the epithelial cells of the intestine and interacts with APOBEC1 and A1CF. RBM47 can replace A1CF and is sufficient with APOBEC1 for C to U RNA editing. C to U editing of Apob and other RNA is impaired in Rbm47-deficient mice. The RNA-binding protein RBM47 is required for normal Cytidine to Uridine RNA editing in mice and is sufficient for the C to U editing activity of APOBEC1, indicating that the composition of the editosome holoenzyme needs to be revised.

AB - Cytidine (C) to Uridine (U) RNA editing is a post-transcriptional modification that is accomplished by the deaminase APOBEC1 and its partnership with the RNA-binding protein A1CF. We identify and characterise here a novel RNA-binding protein, RBM47, that interacts with APOBEC1 and A1CF and is expressed in tissues where C to U RNA editing occurs. RBM47 can substitute for A1CF and is necessary and sufficient for APOBEC1-mediated editing in vitro. Editing is further impaired in Rbm47-deficient mutant mice. These findings suggest that RBM47 and APOBEC1 constitute the basic machinery for C to U RNA editing. Synopsis The RNA-binding protein RBM47 is required for normal Cytidine to Uridine RNA editing in mice and is sufficient for the C to U editing activity of APOBEC1, indicating that the composition of the editosome holoenzyme needs to be revised. RBM47 is found in the epithelial cells of the intestine and interacts with APOBEC1 and A1CF. RBM47 can replace A1CF and is sufficient with APOBEC1 for C to U RNA editing. C to U editing of Apob and other RNA is impaired in Rbm47-deficient mice. The RNA-binding protein RBM47 is required for normal Cytidine to Uridine RNA editing in mice and is sufficient for the C to U editing activity of APOBEC1, indicating that the composition of the editosome holoenzyme needs to be revised.

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DO - 10.15252/embr.201438450

M3 - Article

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Fossat N, Tourle K, Radziewic T, Barratt K, Liebhold D, Studdert JB et al. C to U RNA editing mediated by APOBEC1 requires RNA-binding protein RBM47. EMBO Reports. 2014;15(8):903-910. https://doi.org/10.15252/embr.201438450