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The H3 histone chaperone NASP SIM3 escorts CenH3 in Arabidopsis
Author(s) -
Le Goff Samuel,
Keçeli Burcu Nur,
Jeřábková Hana,
Heckmann Stefan,
Rutten Twan,
Cotterell Sylviane,
Schubert Veit,
Roitinger Elisabeth,
Mechtler Karl,
Franklin F. Christopher H.,
Tatout Christophe,
Houben Andreas,
Geelen Danny,
Probst Aline V.,
Lermontova Inna
Publication year - 2020
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.14518
Subject(s) - histone h3 , centromere , microbiology and biotechnology , biology , histone , kinetochore , chaperone (clinical) , arabidopsis , genetics , chromosome , gene , medicine , pathology , mutant
Summary Centromeres define the chromosomal position where kinetochores form to link the chromosome to microtubules during mitosis and meiosis. Centromere identity is determined by incorporation of a specific histone H3 variant termed CenH3. As for other histones, escort and deposition of CenH3 must be ensured by histone chaperones, which handle the non‐nucleosomal CenH3 pool and replenish CenH3 chromatin in dividing cells. Here, we show that the Arabidopsis orthologue of the mammalian NUCLEAR AUTOANTIGENIC SPERM PROTEIN (NASP) and Schizosaccharomyces pombe histone chaperone Sim3 is a soluble nuclear protein that binds the histone variant CenH3 and affects its abundance at the centromeres. NASP SIM3 is co‐expressed with Arabidopsis CenH3 in dividing cells and binds directly to both the N‐terminal tail and the histone fold domain of non‐nucleosomal CenH3. Reduced NASP SIM3 expression negatively affects CenH3 deposition, identifying NASP SIM3 as a CenH3 histone chaperone.