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A short motif in Drosophila SECIS Binding Protein 2 provides differential binding affinity to SECIS RNA hairpins

Mostra el registre parcial de l'element Takeuchi, Akiko Schmitt, David Chapple, Charles E. Babaylova, Elena Karpova, Galina Guigó Serra, Roderic Krol, Alain Allmang, Christine
dc.contributor.other Universitat Pompeu Fabra 2011-11-28T11:08:08Z 2011-11-28T11:08:08Z 2009
dc.identifier.citation Takeuchi A, Schmitt D, Chapple C, Babaylova E, Karpova G, Guigo R, Krol A, Allmang C. A short motif in Drosophila SECIS Binding Protein 2 provides differential binding affinity to SECIS RNA hairpins. Nucleic acids research. 2009; 37(7): 2126-2141. DOI 10.1093/nar/gkp078
dc.identifier.issn 0305-1048
dc.description.abstract 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.
dc.description.sponsorship 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.
dc.language.iso eng
dc.publisher Oxford University Press
dc.rights (c) 2009 The Author(s). This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License ( 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
dc.subject.other Aminoàcids -- Anàlisi
dc.subject.other Proteïnes -- Fixació
dc.subject.other Drosòfila -- Genètica
dc.title A short motif in Drosophila SECIS Binding Protein 2 provides differential binding affinity to SECIS RNA hairpins
dc.type info:eu-repo/semantics/article
dc.subject.keyword 3'UTR
dc.subject.keyword Animals
dc.subject.keyword Selenoproteins
dc.subject.keyword Amino Acid Sequence
dc.subject.keyword Drosophila melanogaster
dc.subject.keyword RNA
dc.subject.keyword Drosophila Proteins
dc.subject.keyword Protein Binding
dc.relation.projectID info:eu-repo/grantAgreement/ES/2PN/BIO2006-03380
dc.relation.projectID info:eu-repo/grantAgreement/EC/FP6/503265
dc.rights.accessRights info:eu-repo/semantics/openAccess
dc.type.version info:eu-repo/semantics/publishedVersion

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