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: | , , , , , , , |
|---|---|
| Tipo de recurso: | artículo |
| Estado: | Versión publicada |
| Fecha de publicación: | 2009 |
| País: | España |
| Institución: | Universitat Pompeu Fabra |
| Repositorio: | Repositorio Digital de la UPF |
| OAI Identifier: | oai:repositori.upf.edu:10230/13150 |
| Acceso en línea: | http://hdl.handle.net/10230/13150 http://dx.doi.org/10.1093/nar/gkp078 |
| Access Level: | acceso abierto |
| Palabra clave: | Aminoàcids -- Anàlisi Proteïnes -- Fixació Drosòfila -- Genètica 3&apos UTR Animals Selenoproteins Amino Acid Sequence Drosophila melanogaster RNA Drosophila Proteins Protein Binding |
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A short motif in Drosophila SECIS Binding Protein 2 provides differential binding affinity to SECIS RNA hairpinsTakeuchi, AkikoSchmitt, DavidChapple, Charles E.Babaylova, ElenaKarpova, GalinaGuigó Serra, RodericKrol, AlainAllmang, ChristineAminoàcids -- AnàlisiProteïnes -- FixacióDrosòfila -- Genètica3&aposUTRAnimalsSelenoproteinsAmino Acid SequenceDrosophila melanogasterRNADrosophila ProteinsProtein BindingSelenoproteins 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.Action Concertée Incitative (BCMS 226) and Programme InterOrganismes (Tox.Nuc-E) [to A.K.]; the Spanish Ministry of Education (BIO2006-03380) and Biosapiens LSHG-CT-2003-503265 (FP6 Programme of the European Commission) [to R.G.]; the Russian Foundation for Basic Research (grant #08-04-00508) [to G.K.]; Pre-doctoral fellowship from the Japanese Ministry of Education, Culture, Sports, Science and Technology [to A.T.]; Pre-doctoral fellowship of the Spanish Ministry of Education and Science [to C.C.]; EMBO short-term fellowship (ASTF 91-2007) [to E.B.]. Funding for open access charge: CNRS.Oxford University Press201120112009info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionapplication/pdfapplication/pdfhttp://hdl.handle.net/10230/13150http://dx.doi.org/10.1093/nar/gkp078reponame:Repositorio Digital de la UPFinstname:Universitat Pompeu FabraInglésNucleic acids research. 2009;37(7):2126-41info:eu-repo/grantAgreement/ES/2PN/BIO2006-03380info:eu-repo/grantAgreement/EC/FP6/503265© 2009 The Author(s). 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. Published article is also available at http://nar.oxfordjournals.org/content/37/7/2126.http://creativecommons.org/licenses/by-nc/2.0/uk/info:eu-repo/semantics/openAccessoai:repositori.upf.edu:10230/131502026-06-12T07:21:37Z |
| dc.title.none.fl_str_mv |
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 |
| spellingShingle |
A short motif in Drosophila SECIS Binding Protein 2 provides differential binding affinity to SECIS RNA hairpins Takeuchi, Akiko Aminoàcids -- Anàlisi Proteïnes -- Fixació Drosòfila -- Genètica 3&apos UTR Animals Selenoproteins Amino Acid Sequence Drosophila melanogaster RNA Drosophila Proteins Protein Binding |
| title_short |
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_sort |
A short motif in Drosophila SECIS Binding Protein 2 provides differential binding affinity to SECIS RNA hairpins |
| dc.creator.none.fl_str_mv |
Takeuchi, Akiko Schmitt, David Chapple, Charles E. Babaylova, Elena Karpova, Galina Guigó Serra, Roderic Krol, Alain Allmang, Christine |
| author |
Takeuchi, Akiko |
| author_facet |
Takeuchi, Akiko Schmitt, David Chapple, Charles E. Babaylova, Elena Karpova, Galina Guigó Serra, Roderic Krol, Alain Allmang, Christine |
| author_role |
author |
| author2 |
Schmitt, David Chapple, Charles E. Babaylova, Elena Karpova, Galina Guigó Serra, Roderic Krol, Alain Allmang, Christine |
| author2_role |
author author author author author author author |
| dc.subject.none.fl_str_mv |
Aminoàcids -- Anàlisi Proteïnes -- Fixació Drosòfila -- Genètica 3&apos UTR Animals Selenoproteins Amino Acid Sequence Drosophila melanogaster RNA Drosophila Proteins Protein Binding |
| topic |
Aminoàcids -- Anàlisi Proteïnes -- Fixació Drosòfila -- Genètica 3&apos UTR Animals Selenoproteins Amino Acid Sequence Drosophila melanogaster RNA Drosophila Proteins Protein Binding |
| 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. |
| publishDate |
2009 |
| dc.date.none.fl_str_mv |
2009 2011 2011 |
| dc.type.none.fl_str_mv |
info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion |
| format |
article |
| status_str |
publishedVersion |
| dc.identifier.none.fl_str_mv |
http://hdl.handle.net/10230/13150 http://dx.doi.org/10.1093/nar/gkp078 |
| url |
http://hdl.handle.net/10230/13150 http://dx.doi.org/10.1093/nar/gkp078 |
| dc.language.none.fl_str_mv |
Inglés |
| language_invalid_str_mv |
Inglés |
| dc.relation.none.fl_str_mv |
Nucleic acids research. 2009;37(7):2126-41 info:eu-repo/grantAgreement/ES/2PN/BIO2006-03380 info:eu-repo/grantAgreement/EC/FP6/503265 |
| dc.rights.none.fl_str_mv |
http://creativecommons.org/licenses/by-nc/2.0/uk/ info:eu-repo/semantics/openAccess |
| rights_invalid_str_mv |
http://creativecommons.org/licenses/by-nc/2.0/uk/ |
| eu_rights_str_mv |
openAccess |
| dc.format.none.fl_str_mv |
application/pdf application/pdf |
| dc.publisher.none.fl_str_mv |
Oxford University Press |
| publisher.none.fl_str_mv |
Oxford University Press |
| dc.source.none.fl_str_mv |
reponame:Repositorio Digital de la UPF instname:Universitat Pompeu Fabra |
| instname_str |
Universitat Pompeu Fabra |
| reponame_str |
Repositorio Digital de la UPF |
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Repositorio Digital de la UPF |
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1869412534493118464 |
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15.81155 |