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The intrinsically disordered C-terminal F domain of the ecdysteroid receptor from Aedes aegypti exhibits metal ion-binding ability.
Autorzy
Rok wydania
2019
Czasopismo
Journal of Steroid Biochemistry and Molecular Biology
Numer woluminu
186
Strony
42-55
DOI
10.1016/j.jsbmb.2018.09.008
Kolekcja
Język
Angielski
Typ publikacji
Artykuł
Streszczenie
The dominant vector of dengue and Zika diseases is a female Aedes aegypti mosquito. Its reproduction is controlled by the formation of an active heterodimer complex of the 20-hydroxyecdysone receptor (EcR) and Ultraspiracle protein (Usp). Although EcR exhibits a structural and functional organization typical of nuclear receptors (NRs), the EcR C-terminus has an additional F domain (AaFEcR) that is rarely present in the NRs superfamily. The presence of F domains is evolutionarily not well conserved in the NRs. The structure-function relationship of EcR F domains in arthropods is unclear and enigmatic. To date, there have been no data concerning the structure and function of AaFEcR.
Our results showed that AaFEcR belongs to a family of intrinsically disordered proteins (IDPs) and possesses putative pre-molten globule (PMG) characteristics. Unexpectedly, additional amino acid composition in silico analyses revealed the presence of short unique repeated Pro-His clusters forming an HGPHPHPHG motif, which is similar to those responsible for Zn2+ and Cu2+ binding in histidine-proline-rich glycoproteins (HPRGs). Using SEC, SV-AUC and ESI-TOF MS, we showed that the intrinsically disordered AaFEcR is able to bind metal ions and form complexes with these ions. Our studies provide new insight into the structural organization and activities of the F domains of NRs. This unique for the F domains of NRs ion-binding propensity demonstrated by the AaFEcR domain may be a part of the ecdysteroid receptor’s mechanism for regulating the expression of genes encoding oxidative stress-protecting proteins.
Słowa kluczowe
Aedes aegypti, Ecdysteroid receptor, Zika and dengue vector, nuclear receptors, Intrinsically disordered proteins
Licencja otwartego dostępu
Licencja ta zezwala na rozpowszechnianie, przedstawianie i wykonywanie utworu jedynie w celach niekomercyjnych oraz pod warunkiem zachowania go w oryginalnej postaci (nie tworzenia utworów zależnych). Jest to najbardziej restrykcyjna z licencji.
Pełny tekst licencji: https://creativecommons.org/licenses/by-nc-nd/4.0/legalcode
Adres publiczny
http://dx.doi.org/10.1016/j.jsbmb.2018.09.008
Strona internetowa wydawcy
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