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Plant J. 2019 Aug 29. doi: 10.1111/tpj.14518. [Epub ahead of print]

The H3 histone chaperone NASPSIM 3 escorts CenH3 in Arabidopsis.

Author information

1
GReD, Université Clermont Auvergne, CNRS, INSERM, BP 38, 63001, Clermont-Ferrand, France.
2
Department of Plants and Crops unit HortiCell, Faculty of Bioscience Engineering, Ghent University Coupure links, 653, 9000, Ghent, Belgium.
3
The Czech Academy of Sciences, Institute of Experimental Botany (IEB), Centre of the Region Haná for Biotechnological and Agricultural Research, Slechtitelu 31, 783 71, Olomouc, Czech Republic.
4
Leibniz Institute of Plant Genetics and Crop Plant Research (IPK) Gatersleben, Corrensstrasse 3, D-06466, Seeland, Germany.
5
Institute of Molecular Pathology (IMP), Vienna BioCenter (VBC), Vienna, 1030, Austria.
6
Institute of Molecular Biotechnology (IMBA), Austrian Academy of Sciences, Vienna BioCenter (VBC), Vienna, 1030, Austria.
7
Gregor Mendel Institute (GMI), Austrian Academy of Sciences, Vienna BioCenter (VBC), Vienna, 1030, Austria.
8
School of Biosciences, University of Birmingham, Edgbaston, Birmingham, B15 2TT, UK.
9
Mendel Centre for Plant Genomics and Proteomics, CEITEC, Masaryk University, Brno, CZ-62500, Czech Republic.

Abstract

Centromeres define the chromosomal position where kinetochores form to link the chromosome to microtubules during mitosis and meiosis. Centromere identity is determined by incorporation of a specific histone H3 variant termed CenH3. As for other histones, escort and deposition of CenH3 must be ensured by histone chaperones, which handle the non-nucleosomal CenH3 pool and replenish CenH3 chromatin in dividing cells. Here, we show that the Arabidopsis orthologue of the mammalian NUCLEAR AUTOANTIGENIC SPERM PROTEIN (NASP) and S. pombe histone chaperone Sim3 is a soluble nuclear protein that binds the histone variant CenH3 and affects its abundance at the centromeres. NASPSIM 3 is co-expressed with Arabidopsis CenH3 in dividing cells and binds directly to both the N-terminal tail and the histone fold domain of non-nucleosomal CenH3. Reduced NASPSIM 3 expression negatively affects CenH3 deposition, identifying NASPSIM 3 as a CenH3 histone chaperone. This article is protected by copyright. All rights reserved.

KEYWORDS:

Arabidopsis thaliana ; NASPSIM 3 ; CenH3; centromere; histone chaperone; kinetochore

PMID:
31463991
DOI:
10.1111/tpj.14518

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