| Literature DB >> 31463991 |
Samuel Le Goff1, Burcu Nur Keçeli2, Hana Jeřábková3, Stefan Heckmann4, Twan Rutten4, Sylviane Cotterell1, Veit Schubert4, Elisabeth Roitinger5,6,7, Karl Mechtler5,6,7, F Christopher H Franklin8, Christophe Tatout1, Andreas Houben4, Danny Geelen2, Aline V Probst1, Inna Lermontova4,9.
Abstract
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. NASPSIM3 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 NASPSIM3 expression negatively affects CenH3 deposition, identifying NASPSIM3 as a CenH3 histone chaperone.Entities:
Keywords: zzm321990Arabidopsis thalianazzm321990; CenH3; NASPSIM3; centromere; histone chaperone; kinetochore
Year: 2019 PMID: 31463991 DOI: 10.1111/tpj.14518
Source DB: PubMed Journal: Plant J ISSN: 0960-7412 Impact factor: 6.417