Deregulated Phosphorylation of CENH3 at Ser65 Affects the Development of Floral Meristems in Arabidopsis thaliana

0507848 - ÚEB 2020 RIV CH eng J - Journal Article
Demidov, D. - Heckmann, S. - Weiss, O. - Rutten, T. - Tomaštíková, Eva - Kuhlmann, M. - Scholl, P. - Municio, C. M. - Lermontova, I. - Houben, A.
Deregulated Phosphorylation of CENH3 at Ser65 Affects the Development of Floral Meristems in Arabidopsis thaliana.
Frontiers in Plant Science. Roč. 10, JUL 25 (2019), č. článku 928. ISSN 1664-462X. E-ISSN 1664-462X
R&D Projects: GA MŠMT(CZ) LO1204; GA MŠMT(CZ) EF16_019/0000827
Institutional support: RVO:61389030
Keywords : aurora-b kinase * histone h3 * chromosome segregation * centromeric chromatin * protein * deposition * identification * expression * division * dynamics * cenh3 * phosphorylation * Aurora kinase * floral meristem * Arabidopsis
OECD category: Biochemistry and molecular biology
Impact factor: 4.402, year: 2019
Method of publishing: Open access
http://dx.doi.org/10.3389/fpls.2019.00928

Several histone variants are posttranslationally phosphorylated. Little is known about phosphorylation of the centromere-specific histone 3 (CENH3) variant in plants. We show that CENH3 of Arabidopsis thaliana is phosphorylated in vitro by Aurora3, predominantly at serine 65. Interaction of Aurora3 and CENH3 was found by immunoprecipitation (IP) in A. thaliana and by bimolecular fluorescence complementation. Western blotting with an anti-CENH3 pS65 antibody showed that CENH3 pS65 is more abundant in flower buds than elsewhere in the plant. Substitution of serine 65 by either alanine or aspartic acid resulted in a range of phenotypic abnormalities, especially in reproductive tissues. We conclude that Aurora3 phosphorylates CENH3 at S65 and that this post-translational modification is required for the proper development of the floral meristem.
Permanent Link: http://hdl.handle.net/11104/0298809