期刊
JOURNAL OF MOLECULAR BIOLOGY
卷 427, 期 10, 页码 1949-1963出版社
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/j.jmb.2015.03.010
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资金
- Wellcome Trust [082010/Z/07/Z]
- Engineering and Physical Sciences Research Council [GR/R99393/01, EP/C015452/1]
- European Union [RII3-CT-2003-505925]
- Keele University
- Medical Research Council
- Cancer Research UK
- Wellcome Trust Fellowship [092441/Z/10/Z]
- Harmonia 5 Grant from the Polish National Science Center [2013/10/M/NZ2/00298]
- Wellcome Trust [082010/Z/07/Z, 092441/Z/10/Z] Funding Source: Wellcome Trust
- EPSRC [EP/C015452/1] Funding Source: UKRI
- Cancer Research UK [11431] Funding Source: researchfish
- Engineering and Physical Sciences Research Council [GR/R99393/01, EP/C015452/1] Funding Source: researchfish
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 dinner 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. (C) 2015 The Authors. Published by Elsevier Ltd. This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).
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