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The H3 chaperone function of NASP is conserved in Arabidopsis.
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2016 (English)In: The Plant Journal, ISSN 0960-7412, E-ISSN 1365-313XArticle in journal (Refereed) Epub ahead of print
Abstract [en]

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.

Place, publisher, year, edition, pages
2016.
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Natural Sciences
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URN: urn:nbn:se:uu:diva-306195DOI: 10.1111/tpj.13263PubMedID: 27402088OAI: oai:DiVA.org:uu-306195DiVA: diva2:1040054
Available from: 2016-10-26 Created: 2016-10-26 Last updated: 2016-10-26

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Ramström, Margareta
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