The H3 chaperone function of NASP is conserved in Arabidopsis |
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| Authors: | Vladimir Maksimov Miyuki Nakamura Thomas Wildhaber Paolo Nanni Margareta Ramström Jonas Bergquist Lars Hennig |
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| Institution: | 1. Department of Plant Biology and Linnean Center for Plant Biology, Swedish University of Agricultural Sciences, Uppsala, Sweden;2. Department of Biology and Zurich‐Basel Plant Science Center, ETH Zurich, Zurich, Switzerland;3. Functional Genomics Center Zurich, University of Zurich/ETH Zurich, Zurich, Switzerland;4. Department of Chemistry‐BMC, Analytical Chemistry and Science for Life Laboratory, Uppsala University, Uppsala, Sweden |
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| 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 in vitro 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 in vitro. Arabidopsis NASP promotes H3–H4]2 tetrasome formation, possibly by providing preassembled histone tetramers. However, NASP does not promote disassembly of in vitro 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. |
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| Keywords: | histone chaperone chromatin nucleosome
Arabidopsis thaliana
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