dc.contributor.author | Lazzaretti, D | |
dc.contributor.author | Veith, K | |
dc.contributor.author | Kramer, K | |
dc.contributor.author | Basquin, C | |
dc.contributor.author | Urlaub, H | |
dc.contributor.author | Irion, U | |
dc.contributor.author | Bono, F | |
dc.date.accessioned | 2018-11-14T14:59:52Z | |
dc.date.issued | 2016-07-04 | |
dc.description.abstract | Anterior patterning in Drosophila is mediated by the localization of bicoid (bcd) mRNA at the anterior pole of the oocyte. Exuperantia (Exu) is a putative exonuclease (EXO) associated with bcd and required for its localization. We present the crystal structure of Exu, which reveals a dimeric assembly with each monomer consisting of a 3'-5' EXO-like domain and a sterile alpha motif (SAM)-like domain. The catalytic site is degenerate and inactive. Instead, the EXO-like domain mediates dimerization and RNA binding. We show that Exu binds RNA directly in vitro, that the SAM-like domain is required for RNA binding activity and that Exu binds a structured element present in the bcd 3' untranslated region with high affinity. Through structure-guided mutagenesis, we show that Exu dimerization is essential for bcd localization. Our data demonstrate that Exu is a noncanonical RNA-binding protein with EXO-SAM-like domain architecture that interacts with its target RNA as a homodimer. | en_GB |
dc.description.sponsorship | This project received funding from the Max Planck Gesellschaft, the European Research Council under the European Union's Seventh Framework Programme (FP7/2007-2013), ERC grant agreement no. 310957 and the Deutsche Forschungsgemeinschaft (SFB860 to K.K. and H.U., and BO3588/2-1 to F.B.). | en_GB |
dc.identifier.citation | Vol. 23, pp. 705 - 713 | en_GB |
dc.identifier.doi | 10.1038/nsmb.3254 | |
dc.identifier.uri | http://hdl.handle.net/10871/34769 | |
dc.language.iso | en | en_GB |
dc.publisher | Nature Research | en_GB |
dc.relation.url | https://www.ncbi.nlm.nih.gov/pubmed/27376588 | en_GB |
dc.subject | Animals | en_GB |
dc.subject | Catalytic Domain | en_GB |
dc.subject | Crystallography, X-Ray | en_GB |
dc.subject | Drosophila Proteins | en_GB |
dc.subject | Drosophila melanogaster | en_GB |
dc.subject | Egg Proteins | en_GB |
dc.subject | Exonucleases | en_GB |
dc.subject | Female | en_GB |
dc.subject | Homeodomain Proteins | en_GB |
dc.subject | Hydrogen Bonding | en_GB |
dc.subject | Hydrophobic and Hydrophilic Interactions | en_GB |
dc.subject | Models, Molecular | en_GB |
dc.subject | Nucleic Acid Conformation | en_GB |
dc.subject | Protein Binding | en_GB |
dc.subject | Protein Interaction Domains and Motifs | en_GB |
dc.subject | Protein Multimerization | en_GB |
dc.subject | Protein Structure, Quaternary | en_GB |
dc.subject | Protein Transport | en_GB |
dc.subject | RNA | en_GB |
dc.subject | RNA-Binding Proteins | en_GB |
dc.subject | Trans-Activators | en_GB |
dc.title | The bicoid mRNA localization factor Exuperantia is an RNA-binding pseudonuclease. | en_GB |
dc.type | Article | en_GB |
dc.date.available | 2018-11-14T14:59:52Z | |
dc.identifier.issn | 1545-9993 | |
exeter.place-of-publication | United States | en_GB |
dc.description | This is the author accepted manuscript. | en_GB |
dc.description | Final version available from Nature Research via the DOI in this record. | en_GB |
dc.identifier.journal | Nature Structural and Molecular Biology | en_GB |