The Pentameric Nucleoplasmin Fold Is Present in Drosophila FKBP39 and a Large Number of Chromatin-Related Proteins
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Authors
Edlich-Muth, Christian
Artero, Jean-Baptiste
Callow, Phil
Przewloka, Marcin R
Watson, Aleksandra
Zhang, Wei
Debski, Janusz
Dadlez, Michal
Round, Adam R
Forsyth, V Trevor
Publication Date
2015-03-24Journal Title
Journal of Molecular Biology
ISSN
0022-2836
Publisher
Elsevier
Volume
427
Pages
1949-1963
Language
English
Type
Article
Metadata
Show full item recordCitation
Edlich-Muth, C., Artero, J., Callow, P., Przewloka, M. R., Watson, A., Zhang, W., Glover, D., et al. (2015). The Pentameric Nucleoplasmin Fold Is Present in Drosophila FKBP39 and a Large Number of Chromatin-Related Proteins. Journal of Molecular Biology, 427 1949-1963. https://doi.org/10.1016/j.jmb.2015.03.010
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.
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Keywords
histone chaperone, nucleoplasmin, FKBP, structure determination, NMR
Sponsorship
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 European Molecular Biology Laboratory Hamburg outstation (EMBL-HH) for the provision of beamtime and access to the experimental facilities of D22, ID14eh3 and X33 respectively. We would also like to thank the local contacts at all the facilities for providing assistance in using the beam lines.
Funder references
Wellcome Trust (082010/Z/07/Z)
Wellcome Trust (092441/Z/10/Z)
Cancer Research UK (11431)
Identifiers
External DOI: https://doi.org/10.1016/j.jmb.2015.03.010
This record's URL: https://www.repository.cam.ac.uk/handle/1810/247881
Rights
Attribution 2.0 UK: England & Wales
Licence URL: http://creativecommons.org/licenses/by/2.0/uk/
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