title: The pentameric nucleoplasmin fold is present in Drosophila FKBP39 and a large number of chromatin-related proteins.
abstract: Nucleoplasmin is a histone chaperone that consists of a pentameric N-terminal domain and an unstructured C-terminal tail. The pentameric core domain, a doughnut-like structure with a central pore, is only found in the nucleoplasmin family. Here, we report the first structure of a nucleoplasmin-like domain (NPL) from the unrelated Drosophila protein, FKBP39, and we present evidence that this protein associates with chromatin. Furthermore, we show that two other chromatin proteins, Arabidopsis thaliana histone deacetylase type 2 (HD2) and Saccharomyces cerevisiae Fpr4, share the NPL fold and form pentamers, or a dimer of pentamers in the case of HD2. Thus, we propose a new family of proteins that share the pentameric nucleoplasmin-like NPL domain and are found in protists, fungi, plants and animals.
authors: Department of Biochemistry, University of Cambridge, 80 Tennis Court Road, CB2 1GA Cambridge, United Kingdom.
authors: Christian
authors: C
authors: Edlich-Muth
authors: Life Sciences Group, Institut Laue-Langevin, 71 Avenue des Martyrs, CS 20156, Grenoble, Cedex 9, France; Faculty of Natural Sciences, Keele University, ST5 5BG Staffordshire, United Kingdom.
authors: Jean-Baptiste
authors: JB
authors: Artero
authors: Life Sciences Group, Institut Laue-Langevin, 71 Avenue des Martyrs, CS 20156, Grenoble, Cedex 9, France; Faculty of Natural Sciences, Keele University, ST5 5BG Staffordshire, United Kingdom.
authors: Phil
authors: P
authors: Callow
authors: Department of Genetics, University of Cambridge, Downing Street, CB2 3EH Cambridge, United Kingdom.
authors: Marcin R
authors: MR
authors: Przewloka
authors: Department of Biochemistry, University of Cambridge, 80 Tennis Court Road, CB2 1GA Cambridge, United Kingdom.
authors: Aleksandra A
authors: AA
authors: Watson
authors: Department of Biochemistry, University of Cambridge, 80 Tennis Court Road, CB2 1GA Cambridge, United Kingdom.
authors: Wei
authors: W
authors: Zhang
authors: Department of Genetics, University of Cambridge, Downing Street, CB2 3EH Cambridge, United Kingdom.
authors: David M
authors: DM
authors: Glover
authors: Mass Spectrometry Laboratory, Department of Biophysics, Institute of Biochemistry and Biophysics, Polish Academy of Sciences, 5A Pawinskiego Street, 02-106 Warsaw, Poland.
authors: Janusz
authors: J
authors: Debski
authors: Mass Spectrometry Laboratory, Department of Biophysics, Institute of Biochemistry and Biophysics, Polish Academy of Sciences, 5A Pawinskiego Street, 02-106 Warsaw, Poland.
authors: Michal
authors: M
authors: Dadlez
authors: European Molecular Biology Laboratory, Grenoble Outstation, 71 Avenue des Martyrs, 38042 Grenoble, France; Unit for Virus Host-Cell Interactions, University Grenoble Alpes-European Molecular Biology Laboratory-CNRS, 71 Avenue des Martyrs, 38042 Grenoble, France; Faculty of Natural Sciences, Keele University, ST5 5BG Staffordshire, United Kingdom.
authors: Adam R
authors: AR
authors: Round
authors: Life Sciences Group, Institut Laue-Langevin, 71 Avenue des Martyrs, CS 20156, Grenoble, Cedex 9, France; Faculty of Natural Sciences, Keele University, ST5 5BG Staffordshire, United Kingdom.
authors: V Trevor
authors: VT
authors: Forsyth
authors: Department of Biochemistry, University of Cambridge, 80 Tennis Court Road, CB2 1GA Cambridge, United Kingdom. Electronic address: e.d.laue@bioc.cam.ac.uk.
authors: Ernest D
authors: ED
authors: Laue
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D017360:Arabidopsis / Q000378:metabolism; D002843:Chromatin / Q000378:metabolism*; D003432:Cross-Linking Reagents; D018360:Crystallography, X-Ray; D029721:Drosophila Proteins / Q000737:chemistry* / Q000378:metabolism; D004331:Drosophila melanogaster / Q000378:metabolism; D056488:Histone Chaperones / Q000737:chemistry* / Q000378:metabolism; D056464:Histone Deacetylase 2 / Q000737:chemistry* / Q000378:metabolism; D006657:Histones / Q000378:metabolism*; D047468:Immunoprecipitation; D008958:Models, Molecular; D008969:Molecular Sequence Data; D056489:Nucleoplasmins / Q000737:chemistry* / Q000378:metabolism; D010802:Phylogeny; D011485:Protein Binding; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D011994:Recombinant Proteins / Q000737:chemistry* / Q000378:metabolism; D012441:Saccharomyces cerevisiae / Q000378:metabolism; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry* / Q000378:metabolism; D017386:Sequence Homology, Amino Acid; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; D013329:Structure-Activity Relationship; D022021:Tacrolimus Binding Proteins / Q000737:chemistry* / Q000378:metabolism
chemical_list: D002843:Chromatin; D003432:Cross-Linking Reagents; D029721:Drosophila Proteins; C093658:FKBP39 protein, Drosophila; D056488:Histone Chaperones; D006657:Histones; D056489:Nucleoplasmins; D011994:Recombinant Proteins; D029701:Saccharomyces cerevisiae Proteins; D056464:Histone Deacetylase 2; D022021:Tacrolimus Binding Proteins; C513494:Fpr4 protein, S cerevisiae
keywords: FKBP; NMR; histone chaperone; nucleoplasmin; structure determination