A structural signature motif enlightens the origin and diversification of nuclear receptors
Autoři:
Brice Beinsteiner aff001; Gabriel V. Markov aff005; Stéphane Erb aff006; Yassmine Chebaro aff001; Alastair G. McEwen aff001; Sarah Cianférani aff006; Vincent Laudet aff007; Dino Moras aff001; Isabelle M. L. Billas aff001
Působiště autorů:
IGBMC (Institute of Genetics and of Molecular and Cellular Biology), Illkirch, France
aff001; Université de Strasbourg, Unistra, Strasbourg, France
aff002; Institut National de la Santé et de la Recherche Médicale (INSERM) U1258, Illkirch, France
aff003; Centre National de la Recherche Scientifique (CNRS) UMR 7104, Illkirch, France
aff004; Sorbonne Université, CNRS, UMR 8227, Integrative Biology of Marine Models, (LBI2M, UMR8227), Station Biologique de Roscoff (SBR), Roscoff, France
aff005; Laboratoire de Spectrométrie de Masse BioOrganique, Université de Strasbourg, CNRS, IPHC UMR 7178, Strasbourg, France
aff006; Marine Eco-Evo-Devo Unit. Okinawa Institute of Science and Technology, Onna-son, Okinawa, Japan
aff007
Vyšlo v časopise:
A structural signature motif enlightens the origin and diversification of nuclear receptors. PLoS Genet 17(4): e1009492. doi:10.1371/journal.pgen.1009492
Kategorie:
Research Article
doi:
https://doi.org/10.1371/journal.pgen.1009492
Souhrn
Nuclear receptors are ligand-activated transcription factors that modulate gene regulatory networks from embryonic development to adult physiology and thus represent major targets for clinical interventions in many diseases. Most nuclear receptors function either as homodimers or as heterodimers. The dimerization is crucial for gene regulation by nuclear receptors, by extending the repertoire of binding sites in the promoters or the enhancers of target genes via combinatorial interactions. Here, we focused our attention on an unusual structural variation of the α-helix, called π-turn that is present in helix H7 of the ligand-binding domain of RXR and HNF4. By tracing back the complex evolutionary history of the π-turn, we demonstrate that it was present ancestrally and then independently lost in several nuclear receptor lineages. Importantly, the evolutionary history of the π-turn motif is parallel to the evolutionary diversification of the nuclear receptor dimerization ability from ancestral homodimers to derived heterodimers. We then carried out structural and biophysical analyses, in particular through point mutation studies of key RXR signature residues and showed that this motif plays a critical role in the network of interactions stabilizing homodimers. We further showed that the π-turn was instrumental in allowing a flexible heterodimeric interface of RXR in order to accommodate multiple interfaces with numerous partners and critical for the emergence of high affinity receptors. Altogether, our work allows to identify a functional role for the π-turn in oligomerization of nuclear receptors and reveals how this motif is linked to the emergence of a critical biological function. We conclude that the π-turn can be viewed as a structural exaptation that has contributed to enlarging the functional repertoire of nuclear receptors.
Klíčová slova:
Crystal structure – Dimerization – Dimers – Electron density – Evolutionary adaptation – Monomers – Phylogenetic analysis – Sequence motif analysis
Zdroje
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