Structure of SRSF1 RRM1 bound to RNA reveals an unexpected bimodal mode of interaction and explains its involvement in SMN1 exon7 splicing

SRSF1 is an oncoprotein that plays important roles in RNA metabolism. We reveal the structure of the human SRSF1 RRM1 bound to RNA, and propose a bimodal mode of interaction of the protein with RNA. A single mutation in RRM1 changed SRSF1 specificity for RNA and made it active on SMN2 exon7 splicing...

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Autores principales: Antoine Cléry, Miroslav Krepl, Cristina K. X. Nguyen, Ahmed Moursy, Hadi Jorjani, Maria Katsantoni, Michal Okoniewski, Nitish Mittal, Mihaela Zavolan, Jiri Sponer, Frédéric H.-T. Allain
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Lenguaje:EN
Publicado: Nature Portfolio 2021
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Acceso en línea:https://doaj.org/article/f3116688ba6245dbbc7d39591d69df23
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spelling oai:doaj.org-article:f3116688ba6245dbbc7d39591d69df232021-12-02T13:51:03ZStructure of SRSF1 RRM1 bound to RNA reveals an unexpected bimodal mode of interaction and explains its involvement in SMN1 exon7 splicing10.1038/s41467-020-20481-w2041-1723https://doaj.org/article/f3116688ba6245dbbc7d39591d69df232021-01-01T00:00:00Zhttps://doi.org/10.1038/s41467-020-20481-whttps://doaj.org/toc/2041-1723SRSF1 is an oncoprotein that plays important roles in RNA metabolism. We reveal the structure of the human SRSF1 RRM1 bound to RNA, and propose a bimodal mode of interaction of the protein with RNA. A single mutation in RRM1 changed SRSF1 specificity for RNA and made it active on SMN2 exon7 splicing.Antoine CléryMiroslav KreplCristina K. X. NguyenAhmed MoursyHadi JorjaniMaria KatsantoniMichal OkoniewskiNitish MittalMihaela ZavolanJiri SponerFrédéric H.-T. AllainNature PortfolioarticleScienceQENNature Communications, Vol 12, Iss 1, Pp 1-12 (2021)
institution DOAJ
collection DOAJ
language EN
topic Science
Q
spellingShingle Science
Q
Antoine Cléry
Miroslav Krepl
Cristina K. X. Nguyen
Ahmed Moursy
Hadi Jorjani
Maria Katsantoni
Michal Okoniewski
Nitish Mittal
Mihaela Zavolan
Jiri Sponer
Frédéric H.-T. Allain
Structure of SRSF1 RRM1 bound to RNA reveals an unexpected bimodal mode of interaction and explains its involvement in SMN1 exon7 splicing
description SRSF1 is an oncoprotein that plays important roles in RNA metabolism. We reveal the structure of the human SRSF1 RRM1 bound to RNA, and propose a bimodal mode of interaction of the protein with RNA. A single mutation in RRM1 changed SRSF1 specificity for RNA and made it active on SMN2 exon7 splicing.
format article
author Antoine Cléry
Miroslav Krepl
Cristina K. X. Nguyen
Ahmed Moursy
Hadi Jorjani
Maria Katsantoni
Michal Okoniewski
Nitish Mittal
Mihaela Zavolan
Jiri Sponer
Frédéric H.-T. Allain
author_facet Antoine Cléry
Miroslav Krepl
Cristina K. X. Nguyen
Ahmed Moursy
Hadi Jorjani
Maria Katsantoni
Michal Okoniewski
Nitish Mittal
Mihaela Zavolan
Jiri Sponer
Frédéric H.-T. Allain
author_sort Antoine Cléry
title Structure of SRSF1 RRM1 bound to RNA reveals an unexpected bimodal mode of interaction and explains its involvement in SMN1 exon7 splicing
title_short Structure of SRSF1 RRM1 bound to RNA reveals an unexpected bimodal mode of interaction and explains its involvement in SMN1 exon7 splicing
title_full Structure of SRSF1 RRM1 bound to RNA reveals an unexpected bimodal mode of interaction and explains its involvement in SMN1 exon7 splicing
title_fullStr Structure of SRSF1 RRM1 bound to RNA reveals an unexpected bimodal mode of interaction and explains its involvement in SMN1 exon7 splicing
title_full_unstemmed Structure of SRSF1 RRM1 bound to RNA reveals an unexpected bimodal mode of interaction and explains its involvement in SMN1 exon7 splicing
title_sort structure of srsf1 rrm1 bound to rna reveals an unexpected bimodal mode of interaction and explains its involvement in smn1 exon7 splicing
publisher Nature Portfolio
publishDate 2021
url https://doaj.org/article/f3116688ba6245dbbc7d39591d69df23
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