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A short motif in Drosophila SECIS Binding Protein 2 provides differential binding affinity to SECIS RNA hairpins
Selenoproteins contain the amino acid selenocysteine which is encoded by a UGA Sec codon. Recoding UGA Sec requires a complex mechanism, comprising the cis-acting SECIS RNA hairpin in the 3′UTR of selenoprotein mRNAs, and trans-acting factors. Among these, the SECIS Binding Protein 2 (SBP2) is centr...
Autores principales: | , , , , , , , |
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Formato: | Texto |
Lenguaje: | English |
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Oxford University Press
2009
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2673426/ https://www.ncbi.nlm.nih.gov/pubmed/19223320 http://dx.doi.org/10.1093/nar/gkp078 |
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author | Takeuchi, Akiko Schmitt, David Chapple, Charles Babaylova, Elena Karpova, Galina Guigo, Roderic Krol, Alain Allmang, Christine |
author_facet | Takeuchi, Akiko Schmitt, David Chapple, Charles Babaylova, Elena Karpova, Galina Guigo, Roderic Krol, Alain Allmang, Christine |
author_sort | Takeuchi, Akiko |
collection | PubMed |
description | Selenoproteins contain the amino acid selenocysteine which is encoded by a UGA Sec codon. Recoding UGA Sec requires a complex mechanism, comprising the cis-acting SECIS RNA hairpin in the 3′UTR of selenoprotein mRNAs, and trans-acting factors. Among these, the SECIS Binding Protein 2 (SBP2) is central to the mechanism. SBP2 has been so far functionally characterized only in rats and humans. In this work, we report the characterization of the Drosophila melanogaster SBP2 (dSBP2). Despite its shorter length, it retained the same selenoprotein synthesis-promoting capabilities as the mammalian counterpart. However, a major difference resides in the SECIS recognition pattern: while human SBP2 (hSBP2) binds the distinct form 1 and 2 SECIS RNAs with similar affinities, dSBP2 exhibits high affinity toward form 2 only. In addition, we report the identification of a K (lysine)-rich domain in all SBP2s, essential for SECIS and 60S ribosomal subunit binding, differing from the well-characterized L7Ae RNA-binding domain. Swapping only five amino acids between dSBP2 and hSBP2 in the K-rich domain conferred reversed SECIS-binding properties to the proteins, thus unveiling an important sequence for form 1 binding. |
format | Text |
id | pubmed-2673426 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2009 |
publisher | Oxford University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-26734262009-05-15 A short motif in Drosophila SECIS Binding Protein 2 provides differential binding affinity to SECIS RNA hairpins Takeuchi, Akiko Schmitt, David Chapple, Charles Babaylova, Elena Karpova, Galina Guigo, Roderic Krol, Alain Allmang, Christine Nucleic Acids Res RNA Selenoproteins contain the amino acid selenocysteine which is encoded by a UGA Sec codon. Recoding UGA Sec requires a complex mechanism, comprising the cis-acting SECIS RNA hairpin in the 3′UTR of selenoprotein mRNAs, and trans-acting factors. Among these, the SECIS Binding Protein 2 (SBP2) is central to the mechanism. SBP2 has been so far functionally characterized only in rats and humans. In this work, we report the characterization of the Drosophila melanogaster SBP2 (dSBP2). Despite its shorter length, it retained the same selenoprotein synthesis-promoting capabilities as the mammalian counterpart. However, a major difference resides in the SECIS recognition pattern: while human SBP2 (hSBP2) binds the distinct form 1 and 2 SECIS RNAs with similar affinities, dSBP2 exhibits high affinity toward form 2 only. In addition, we report the identification of a K (lysine)-rich domain in all SBP2s, essential for SECIS and 60S ribosomal subunit binding, differing from the well-characterized L7Ae RNA-binding domain. Swapping only five amino acids between dSBP2 and hSBP2 in the K-rich domain conferred reversed SECIS-binding properties to the proteins, thus unveiling an important sequence for form 1 binding. Oxford University Press 2009-04 2009-02-17 /pmc/articles/PMC2673426/ /pubmed/19223320 http://dx.doi.org/10.1093/nar/gkp078 Text en © 2009 The Author(s) http://creativecommons.org/licenses/by-nc/2.0/uk/ This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | RNA Takeuchi, Akiko Schmitt, David Chapple, Charles Babaylova, Elena Karpova, Galina Guigo, Roderic Krol, Alain Allmang, Christine A short motif in Drosophila SECIS Binding Protein 2 provides differential binding affinity to SECIS RNA hairpins |
title | A short motif in Drosophila SECIS Binding Protein 2 provides differential binding affinity to SECIS RNA hairpins |
title_full | A short motif in Drosophila SECIS Binding Protein 2 provides differential binding affinity to SECIS RNA hairpins |
title_fullStr | A short motif in Drosophila SECIS Binding Protein 2 provides differential binding affinity to SECIS RNA hairpins |
title_full_unstemmed | A short motif in Drosophila SECIS Binding Protein 2 provides differential binding affinity to SECIS RNA hairpins |
title_short | A short motif in Drosophila SECIS Binding Protein 2 provides differential binding affinity to SECIS RNA hairpins |
title_sort | short motif in drosophila secis binding protein 2 provides differential binding affinity to secis rna hairpins |
topic | RNA |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2673426/ https://www.ncbi.nlm.nih.gov/pubmed/19223320 http://dx.doi.org/10.1093/nar/gkp078 |
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