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The H3 chaperone function of NASP is conserved in Arabidopsis
Author(s) -
Maksimov Vladimir,
Nakamura Miyuki,
Wildhaber Thomas,
Nanni Paolo,
Ramström Margareta,
Bergquist Jonas,
Hennig Lars
Publication year - 2016
Publication title -
the plant journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.058
H-Index - 269
eISSN - 1365-313X
pISSN - 0960-7412
DOI - 10.1111/tpj.13263
Subject(s) - histone h3 , chaperone (clinical) , histone , arabidopsis , microbiology and biotechnology , chromatin , biology , histone h4 , chemistry , genetics , gene , medicine , pathology , mutant
Summary 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 MSI 1 and a HSC 70 heat shock protein.