دورية أكاديمية

The pentameric nucleoplasmin fold is present in Drosophila FKBP39 and a large number of chromatin-related proteins.

التفاصيل البيبلوغرافية
العنوان: The pentameric nucleoplasmin fold is present in Drosophila FKBP39 and a large number of chromatin-related proteins.
المؤلفون: Edlich-Muth, Christian, Artero, Jean-Baptiste, Callow, Phil, Przewloka, Marcin R, Watson, Aleksandra A, Zhang, Wei, Glover, David M, Debski, Janusz, Dadlez, Michal, Round, Adam R, Forsyth, V Trevor, Laue, Ernest D
بيانات النشر: Academic Press
//dx.doi.org/10.1016/j.jmb.2015.03.010
J Mol Biol
سنة النشر: 2015
المجموعة: Apollo - University of Cambridge Repository
مصطلحات موضوعية: FKBP, NMR, histone chaperone, nucleoplasmin, structure determination, Amino Acid Sequence, Animals, Arabidopsis, Chromatin, Cross-Linking Reagents, Crystallography, X-Ray, Drosophila Proteins, Drosophila melanogaster, Histone Chaperones, Histone Deacetylase 2, Histones, Immunoprecipitation, Models, Molecular, Molecular Sequence Data, Nucleoplasmins, Phylogeny, Protein Binding, Protein Conformation, Protein Structure, Tertiary, Recombinant Proteins, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins
الوصف: 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. ; We are grateful to Gunter Stier for providing the vector; Michael Nilges, Oleg Fedorov, Benjamin Bardiaux, Stefanie Hartmann and Wolfgang Rieping for helpful discussions; and Daniel Nietlispach for NMR expertise. We thank Renato Paro for generously providing us with an anti-FKBP39 antibody. We would like to thank the Wellcome Trust for financial support (grant 082010/Z/07/Z). V.T.F. and E.D.L. acknowledge support from Engineering and Physical Sciences Research Council under grants GR/R99393/01 and EP/C015452/1 for the creation of the Deuteration Laboratory platform operating within the Grenoble Partnership for Structural Biology. V.T.F. also acknowledges support from the European Union under contract RII3-CT-2003-505925. J.B.A. acknowledges the provision of a postdoctoral fellowship held at Keele University. M.R.P. and D.M.G. were supported by the Medical Research Council and Cancer Research UK grants to D.M.G. A.A.W. is a recipient of a Wellcome Trust Fellowship092441/Z/10/Z. J.D. and M.D. were supported by the Harmonia 5 Grant 2013/10/M/NZ2/00298 from the Polish National Science Center. The authors would like to thank the Institut Laue-Langevin (ILL), the European Synchrotron Radiation Facility (ESRF) and the ...
نوع الوثيقة: article in journal/newspaper
وصف الملف: application/pdf
اللغة: English
العلاقة: https://www.repository.cam.ac.uk/handle/1810/247881Test
الإتاحة: https://www.repository.cam.ac.uk/handle/1810/247881Test
حقوق: Attribution 2.0 UK: England & Wales ; http://creativecommons.org/licenses/by/2.0/ukTest/
رقم الانضمام: edsbas.C9FF1F93
قاعدة البيانات: BASE