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Structural basis of IMP3 RRM12 recognition of RNA

The IMP family of RNA binding proteins, also named as insulin-like growth factor 2 (IGF2) mRNA-binding proteins (IGF2BPs), are highly conserved RNA regulators that are involved in many RNA processing stages, including mRNA stability, localization, and translation. There are three paralogs in the IMP...

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Detalles Bibliográficos
Autores principales: Jia, Min, Gut, Heinz, Chao, Jeffrey A.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Cold Spring Harbor Laboratory Press 2018
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6239170/
https://www.ncbi.nlm.nih.gov/pubmed/30135093
http://dx.doi.org/10.1261/rna.065649.118
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author Jia, Min
Gut, Heinz
Chao, Jeffrey A.
author_facet Jia, Min
Gut, Heinz
Chao, Jeffrey A.
author_sort Jia, Min
collection PubMed
description The IMP family of RNA binding proteins, also named as insulin-like growth factor 2 (IGF2) mRNA-binding proteins (IGF2BPs), are highly conserved RNA regulators that are involved in many RNA processing stages, including mRNA stability, localization, and translation. There are three paralogs in the IMP family, IMP1-3, in mammals that all adopt the same domain arrangement with two RNA recognition motifs (RRM) in the N terminus and four KH domains in the C terminus. Here, we report the structure and biochemical characterization of IMP3 RRM12 and its complex with two short RNAs. These structures show that both RRM domains of IMP3 adopt the canonical RRM topology with two α-helices packed on an anti-parallel four stranded β-sheet. The spatial orientation of RRM1 to RRM2 is unique compared with other known tandem RRM structures. In the IMP3 RRM12 complex with RNA, only RRM1 is involved in RNA binding and recognizes a dinucleotide sequence.
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spelling pubmed-62391702019-12-01 Structural basis of IMP3 RRM12 recognition of RNA Jia, Min Gut, Heinz Chao, Jeffrey A. RNA Report The IMP family of RNA binding proteins, also named as insulin-like growth factor 2 (IGF2) mRNA-binding proteins (IGF2BPs), are highly conserved RNA regulators that are involved in many RNA processing stages, including mRNA stability, localization, and translation. There are three paralogs in the IMP family, IMP1-3, in mammals that all adopt the same domain arrangement with two RNA recognition motifs (RRM) in the N terminus and four KH domains in the C terminus. Here, we report the structure and biochemical characterization of IMP3 RRM12 and its complex with two short RNAs. These structures show that both RRM domains of IMP3 adopt the canonical RRM topology with two α-helices packed on an anti-parallel four stranded β-sheet. The spatial orientation of RRM1 to RRM2 is unique compared with other known tandem RRM structures. In the IMP3 RRM12 complex with RNA, only RRM1 is involved in RNA binding and recognizes a dinucleotide sequence. Cold Spring Harbor Laboratory Press 2018-12 /pmc/articles/PMC6239170/ /pubmed/30135093 http://dx.doi.org/10.1261/rna.065649.118 Text en © 2018 Jia et al.; Published by Cold Spring Harbor Laboratory Press for the RNA Society http://creativecommons.org/licenses/by-nc/4.0/ This article is distributed exclusively by the RNA Society for the first 12 months after the full-issue publication date (see http://rnajournal.cshlp.org/site/misc/terms.xhtml). After 12 months, it is available under a Creative Commons License (Attribution-NonCommercial 4.0 International), as described at http://creativecommons.org/licenses/by-nc/4.0/.
spellingShingle Report
Jia, Min
Gut, Heinz
Chao, Jeffrey A.
Structural basis of IMP3 RRM12 recognition of RNA
title Structural basis of IMP3 RRM12 recognition of RNA
title_full Structural basis of IMP3 RRM12 recognition of RNA
title_fullStr Structural basis of IMP3 RRM12 recognition of RNA
title_full_unstemmed Structural basis of IMP3 RRM12 recognition of RNA
title_short Structural basis of IMP3 RRM12 recognition of RNA
title_sort structural basis of imp3 rrm12 recognition of rna
topic Report
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6239170/
https://www.ncbi.nlm.nih.gov/pubmed/30135093
http://dx.doi.org/10.1261/rna.065649.118
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