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Kolonko, M.* ; Bystranowska, D.* ; Taube, M.* ; Kozak, M.* ; Bostock, M.J. ; Popowicz, G.M. ; Ożyhar, A.* ; Greb-Markiewicz, B.*

The intrinsically disordered region of GCE protein adopts a more fixed structure by interacting with the LBD of the nuclear receptor FTZ-F1.

Cell Commun. Signal. 18:180 (2020)
Verlagsversion DOI PMC
Open Access Gold
Creative Commons Lizenzvertrag
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. [MediaObject not available: see fulltext.]
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Publikationstyp Artikel: Journalartikel
Dokumenttyp Wissenschaftlicher Artikel
Korrespondenzautor
Schlagwörter Bhlh-pas Transcription Factor ; C-terminus ; Ftz-f1 ; Germ Cell-expressed Protein ; Intrinsically Disordered Proteins ; Protein-protein Interactions; Small-angle Scattering; Juvenile-hormone Action; Natively Unfolded Proteins; X-ray-scattering; Methoprene-tolerant; Bhlh-pas; Analytical Ultracentrifugation; Sedimentation-velocity; Drosophila; Binding
ISSN (print) / ISBN 1478-811X
e-ISSN 1478-811X
Zeitschrift Cell Communication and Signaling
Quellenangaben Band: 18, Heft: 1, Seiten: , Artikelnummer: 180 Supplement: ,
Verlag BioMed Central
Verlagsort Campus, 4 Crinan St, London N1 9xw, England
Nichtpatentliteratur Publikationen
Begutachtungsstatus Peer reviewed
Institut(e) Institute of Structural Biology (STB)
Förderungen
Polish Ministry of Science and High Education
National Science Centre (NCN)