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Research article - Peer-reviewed, 2016

The H3 chaperone function of NASP is conserved in Arabidopsis

Maksimov, Vladimir; Nakamura, Miyuki; Wildhaber, Thomas; Nanni, Paolo; Ramström, Margareta; Bergquist, Jonas; Hennig, Lars

Abstract

Histones are abundant cellular proteins but, if not incorporated into chromatin, they are usually bound by histone chaperones. Here, we identify Arabidopsis NASP as a chaperone for histones H3.1 and H3.3. NASP interacts invitro with monomeric H3.1 and H3.3 as well as with histone H3.1-H4 and H3.3-H4 dimers. However, NASP does not bind to monomeric H4. NASP shifts the equilibrium between histone dimers and tetramers towards tetramers but does not interact with tetramers invitro. Arabidopsis NASP promotes [H3-H4](2) tetrasome formation, possibly by providing preassembled histone tetramers. However, NASP does not promote disassembly of invitro preassembled tetrasomes. In contrast to its mammalian homolog, Arabidopsis NASP is a predominantly nuclear protein. In vivo, NASP binds mainly monomeric H3.1 and H3.3. Pulldown experiments indicated that NASP may also interact with the histone chaperone MSI1 and a HSC70 heat shock protein.

Keywords

histone; chaperone; chromatin; nucleosome; Arabidopsis thaliana

Published in

Plant Journal
2016, Volume: 88, number: 3, pages: 425-436
Publisher: Wiley-Blackwell

      SLU Authors

      • UKÄ Subject classification

        Cell Biology
        Evolutionary Biology
        Bioinformatics and Systems Biology

        Publication identifier

        DOI: https://doi.org/10.1111/tpj.13263

        Permanent link to this page (URI)

        https://res.slu.se/id/publ/81017