The H3 histone chaperone NASP(SIM3) escorts CenH3 in Arabidopsis

Investor logo

Warning

This publication doesn't include Institute of Computer Science. It includes Central European Institute of Technology. Official publication website can be found on muni.cz.
Authors

LE GOFF S. KECELI B.N. JERABKOVA H. HECKMANN S. RUTTEN T. COTTERELL S. SCHUBERT V. ROITINGER E. MECHTLER E. FRANKLIN F.C.H. TATOUT C. HOUBEN A. GEELEN D. PROBST A.V. LERMONTOVA Inna

Year of publication 2020
Type Article in Periodical
Magazine / Source Plant Journal
MU Faculty or unit

Central European Institute of Technology

Citation
Web https://onlinelibrary.wiley.com/doi/pdfdirect/10.1111/tpj.14518
Doi http://dx.doi.org/10.1111/tpj.14518
Keywords Arabidopsis thaliana; centromere; kinetochore; CenH3; histone chaperone; NASP(SIM3)
Description 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.
Related projects:

You are running an old browser version. We recommend updating your browser to its latest version.

More info