title: Nucleoplasmin-like domain of FKBP39 from Drosophila melanogaster forms a tetramer with partly disordered tentacle-like C-terminal segments.
abstract: Nucleoplasmins are a nuclear chaperone family defined by the presence of a highly conserved N-terminal core domain. X-ray crystallographic studies of isolated nucleoplasmin core domains revealed a β-propeller structure consisting of a set of five monomers that together form a stable pentamer. Recent studies on isolated N-terminal domains from Drosophila 39-kDa FK506-binding protein (FKBP39) and from other chromatin-associated proteins showed analogous, nucleoplasmin-like (NPL) pentameric structures. Here, we report that the NPL domain of the full-length FKBP39 does not form pentameric complexes. Multi-angle light scattering (MALS) and sedimentation equilibrium ultracentrifugation (SE AUC) analyses of the molecular mass of the full-length protein indicated that FKBP39 forms homotetrameric complexes. Molecular models reconstructed from small-angle X-ray scattering (SAXS) revealed that the NPL domain forms a stable, tetrameric core and that FK506-binding domains are linked to it by intrinsically disordered, flexible chains that form tentacle-like segments. Analyses of full-length FKBP39 and its isolated NPL domain suggested that the distal regions of the polypeptide chain influence and determine the quaternary conformation of the nucleoplasmin-like protein. These results provide new insights regarding the conserved structure of nucleoplasmin core domains and provide a potential explanation for the importance of the tetrameric structural organization of full-length nucleoplasmins.
authors.affiliation: Department of Biochemistry, Faculty of Chemistry, Wrocław University of Science and Technology, Wybrzeże Wyspiańskiego 27, 50-370 Wrocław, Poland.
authors.forename: Małgorzata
authors.initials: M
authors.lastname: Kozłowska
authors.affiliation: Department of Biochemistry, Faculty of Chemistry, Wrocław University of Science and Technology, Wybrzeże Wyspiańskiego 27, 50-370 Wrocław, Poland.
authors.forename: Aneta
authors.initials: A
authors.lastname: Tarczewska
authors.affiliation: Department of Biochemistry, Faculty of Chemistry, Wrocław University of Science and Technology, Wybrzeże Wyspiańskiego 27, 50-370 Wrocław, Poland.
authors.forename: Michał
authors.initials: M
authors.lastname: Jakób
authors.affiliation: Department of Biochemistry, Faculty of Chemistry, Wrocław University of Science and Technology, Wybrzeże Wyspiańskiego 27, 50-370 Wrocław, Poland.
authors.forename: Dominika
authors.initials: D
authors.lastname: Bystranowska
authors.affiliation: Department of Macromolecular Physics, Faculty of Physics, Adam Mickiewicz University, Umultowska 85, 61-614 Poznań, Poland.
authors.forename: Michał
authors.initials: M
authors.lastname: Taube
authors.affiliation: Department of Macromolecular Physics, Faculty of Physics, Adam Mickiewicz University, Umultowska 85, 61-614 Poznań, Poland.
authors.forename: Maciej
authors.initials: M
authors.lastname: Kozak
authors.affiliation: International Institute of Molecular and Cell Biology in Warsaw, 02-109 Warszawa, Poland.|Institute of Biochemistry and Biophysics, Polish Academy of Sciences, 02-106 Warszawa, Poland.|Department of Genetics and Biotechnology, Faculty of Biology, University of Warsaw, 02-106 Warszawa, Poland.
authors.forename: Mariusz
authors.initials: M
authors.lastname: Czarnocki-Cieciura
authors.affiliation: Institute of Biochemistry and Biophysics, Polish Academy of Sciences, 02-106 Warszawa, Poland.|Department of Genetics and Biotechnology, Faculty of Biology, University of Warsaw, 02-106 Warszawa, Poland.
authors.forename: Andrzej
authors.initials: A
authors.lastname: Dziembowski
authors.affiliation: Department of Biochemistry, Faculty of Chemistry, Wrocław University of Science and Technology, Wybrzeże Wyspiańskiego 27, 50-370 Wrocław, Poland.
authors.forename: Marek
authors.initials: M
authors.lastname: Orłowski
authors.affiliation: Department of Biochemistry, Faculty of Chemistry, Wrocław University of Science and Technology, Wybrzeże Wyspiańskiego 27, 50-370 Wrocław, Poland.
authors.forename: Katarzyna
authors.initials: K
authors.lastname: Tkocz
authors.affiliation: Department of Biochemistry, Faculty of Chemistry, Wrocław University of Science and Technology, Wybrzeże Wyspiańskiego 27, 50-370 Wrocław, Poland.
authors.forename: Andrzej
authors.initials: A
authors.lastname: Ożyhar
mesh_terms: D000818:Animals; D019540:Area Under Curve; D002942:Circular Dichroism; D029721:Drosophila Proteins / Q000737:chemistry* / Q000378:metabolism*; D004331:Drosophila melanogaster / Q000378:metabolism*; D008958:Models, Molecular; D008970:Molecular Weight; D056489:Nucleoplasmins / Q000378:metabolism*; D000072417:Protein Domains; D055503:Protein Multimerization; D017433:Protein Structure, Secondary; D021381:Protein Transport; D053838:Scattering, Small Angle; D012996:Solutions; D013347:Subcellular Fractions / Q000378:metabolism; D022021:Tacrolimus Binding Proteins / Q000737:chemistry* / Q000378:metabolism*; D014961:X-Ray Diffraction
chemical_list: D029721:Drosophila Proteins; C093658:FKBP39 protein, Drosophila; D056489:Nucleoplasmins; D012996:Solutions; D022021:Tacrolimus Binding Proteins