title: Aurora1 phosphorylation activity on histone H3 and its  cross-talk with other post-translational histone  modifications in Arabidopsis.
abstract: The enzymological properties of AtAurora1, a kinase responsible for the cell cycle-dependent phosphorylation of histone H3 at S10, and its cross-talk with other post-translational histone modifications, were determined. In vitro phosphorylation of H3S10 by AtAurora1 is strongly increased by K9 acetylation, and decreased by K14 acetylation and T11 phosphorylation. However, S10 phosphorylation activity is unaltered by mono-, di- or trimethylation of K9. An interference of H3K9 dimethylation by SUVR4 occurs by a pre-existing phosphorylation at S10. Hence, cross-talk in plants exists between phosphorylation of H3S10 and methylation, acetylation or phosphorylation of neighbouring amino acid residues. AtAurora1 undergoes autophosphorylation in vivo regardless of the presence of substrate, and forms dimers in planta. Of the three ATP-competitive Aurora inhibitors tested, Hesperadin was most effective in reducing the in vivo kinase activity of AtAurora1. Hesperadin consistently inhibited histone H3S10 phosphorylation during mitosis in Arabidopsis cells, but did not affect other H3 post-translational modifications, suggesting a specific inhibition of AtAurora in vivo. Inactivation of AtAurora also caused lagging chromosomes in a number of anaphase cells, but, unlike the situation in mammalian cells, Hesperadin did not influence the microtubule dynamics in dividing cells.
authors: Leibniz Institute of Plant Genetics and Crop Plant Research (IPK), Corrensstrasse 3, 06466 Gatersleben, Germany.
authors: Dmitri
authors: D
authors: Demidov
authors: Susann
authors: S
authors: Hesse
authors: Annegret
authors: A
authors: Tewes
authors: Twan
authors: T
authors: Rutten
authors: Jörg
authors: J
authors: Fuchs
authors: Raheleh Karimi
authors: RK
authors: Ashtiyani
authors: Sandro
authors: S
authors: Lein
authors: Andreas
authors: A
authors: Fischer
authors: Gunter
authors: G
authors: Reuter
authors: Andreas
authors: A
authors: Houben
mesh_terms: D000107:Acetylation; D017360:Arabidopsis / Q000166:cytology / Q000235:genetics / Q000378:metabolism*; D029681:Arabidopsis Proteins / Q000235:genetics / Q000378:metabolism*; D002453:Cell Cycle; D004791:Enzyme Inhibitors / Q000494:pharmacology; D006657:Histones / Q000235:genetics / Q000378:metabolism*; D007211:Indoles / Q000494:pharmacology; D008745:Methylation; D010766:Phosphorylation; D011494:Protein Kinases / Q000235:genetics / Q000378:metabolism*; D011499:Protein Processing, Post-Translational; D011994:Recombinant Proteins / Q000235:genetics / Q000378:metabolism; D013449:Sulfonamides / Q000494:pharmacology
chemical_list: D029681:Arabidopsis Proteins; D004791:Enzyme Inhibitors; D006657:Histones; D007211:Indoles; D011994:Recombinant Proteins; D013449:Sulfonamides; D011494:Protein Kinases; C474723:hesperadin