The intrinsically disordered region of GCE protein adopts a more fixed structure by interacting with the LBD of the nucl
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(2020) 18:180
RESEARCH
Open Access
The intrinsically disordered region of GCE protein adopts a more fixed structure by interacting with the LBD of the nuclear receptor FTZ-F1 Marta Kolonko1* , Dominika Bystranowska1, Michał Taube2, Maciej Kozak2,3, Mark Bostock4,5, Grzegorz Popowicz4,5, Andrzej Ożyhar1 and Beata Greb-Markiewicz1*
Abstract The Drosophila melanogaster Germ cell-expressed protein (GCE) is a paralog of the juvenile hormone (JH) receptor Methoprene tolerant protein (MET). Both proteins mediate JH function, preventing precocious differentiation during D. melanogaster development. Despite that GCE and MET are often referred to as equivalent JH receptors, their functions are not fully redundant and show tissue specificity. Both proteins belong to the family of bHLH-PAS transcription factors. The similarity of their primary structure is limited to defined bHLH and PAS domains, while their long C-terminal fragments (GCEC, METC) show significant differences and are expected to determine differences in GCE and MET protein activities. In this paper we present the structural characterization of GCEC as a coil-like intrinsically disordered protein (IDP) with highly elongated and asymmetric conformation. In comparison to previously characterized METC, GCEC is less compacted, contains more molecular recognition elements (MoREs) and exhibits a higher propensity for induced folding. The NMR shifts perturbation experiment and pull-down assay clearly demonstrated that the GCEC fragment is sufficient to form an interaction interface with the ligand binding domain (LBD) of the nuclear receptor Fushi Tarazu factor-1 (FTZ-F1). Significantly, these interactions can force GCEC to adopt more fixed structure that can modulate the activity, structure and functions of the full-length receptor. The discussed relation of protein functionality with the structural data of inherently disordered GCEC fragment is a novel look at this protein and contributes to a better understanding of the molecular basis of the functions of the C-terminal fragments of the bHLH-PAS family. Keywords: Germ cell-expressed protein, Intrinsically disordered proteins, bHLH-PAS transcription factor, C-terminus, Protein-protein interactions, FTZ-F1
* Correspondence: [email protected]; [email protected] 1 Department of Biochemistry, Molecular Biology and Biotechnology, Faculty of Chemistry, |Wroclaw University of Science and Technology|, Wybrzeze Wyspianskiego 27, 50-370 Wroclaw, Poland Full list of author information is available at the end of the article © The Author(s). 2020 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons li
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