Maksimov, Vladimir
- Department of Plant Biology, Swedish University of Agricultural Sciences
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
Nakamura, Miyuki
- Department of Plant Biology, Swedish University of Agricultural Sciences
- Department of Plant Biology, Swedish University of Agricultural Sciences
Hennig, Lars
- Department of Plant Biology, Swedish University of Agricultural Sciences
- Department of Plant Biology, Swedish University of Agricultural Sciences
UKÄ Subject classification
Cell Biology
Evolutionary Biology
Bioinformatics and Computational Biology (Methods development to be 10203)
Publication identifier
- DOI: https://doi.org/10.1111/tpj.13263
Permanent link to this page (URI)
https://res.slu.se/id/publ/81017