Cell cycle-dependent and lysine residue-specific dynamic changes of histone H4 acetylation in barley
- PMID: 12081372
- DOI: 10.1023/a:1015554124675
Cell cycle-dependent and lysine residue-specific dynamic changes of histone H4 acetylation in barley
Abstract
Histone acetylation affects chromatin conformation and regulates various cellular functions, such as transcription and cell cycle progression. Although mitosis dependent transcriptional silencing and large-scale chromatin structural changes are well established, acetylation of histone H4 during the mitosis is poorly understood in plants. Here, the dynamics of acetylation of histone H4 in defined genome regions has been examined in the fixed barley cells throughout the mitosis by three-dimensional microscopy. Patterns of strong acetylation of the two lysine residues K5 and K16 of histone H4 in the barley genomes were found to be different. In interphase nuclei, H4 acetylated at K 16 was associated with the gene-rich, telomere-associated hemispheres, whereas K5 acetylation was detected in centromeric regions where the heterochromatin is distributed. Regions of strong K5 acetylation changed dynamically as the cell cycle proceeded. At prometaphase, centromeric acetylation at K5 decreased suddenly, with accompanying rapid increases of acetylation in the nucleolar organizing regions (NORs). Reverse changes occurred at telophase. On the other hand, the strongly acetylated regions of the K16 showed changes compatible with transcriptional activities and chromosome condensation throughout the cell cycle. Telomeric acetylation at K16 was detected throughout the cell cycle, although it was reduced at metaphase which corresponds to the most condensed stage of the chromosomes. It is concluded that dynamic changes in H4 acetylation occur in a lysine residue-, stage-, and region-specific manner and that they correlate with changes in the chromosome structure through the cell cycle.
Similar articles
-
Centromere-specific acetylation of histone H4 in barley detected through three-dimensional microscopy.Plant Mol Biol. 2003 Mar;51(4):533-41. doi: 10.1023/a:1022375017938. Plant Mol Biol. 2003. PMID: 12650619
-
Comprehensive analysis of dynamics of histone H4 acetylation in mitotic barley cells.Genes Genet Syst. 2005 Aug;80(4):269-76. doi: 10.1266/ggs.80.269. Genes Genet Syst. 2005. PMID: 16284420
-
Chromatin organization and its relation to replication and histone acetylation during the cell cycle in barley.Chromosoma. 2001 May;110(2):83-92. doi: 10.1007/s004120100132. Chromosoma. 2001. PMID: 11453558
-
Histone acetylation: a possible mechanism for the inheritance of cell memory at mitosis.Bioessays. 1997 Jan;19(1):67-74. doi: 10.1002/bies.950190111. Bioessays. 1997. PMID: 9008418 Review.
-
Dynamics of chromosome positioning during the cell cycle.Curr Opin Cell Biol. 2003 Dec;15(6):664-71. doi: 10.1016/j.ceb.2003.10.014. Curr Opin Cell Biol. 2003. PMID: 14644190 Review.
Cited by
-
Dynamic histone acetylation of late embryonic genes during seed germination.Plant Mol Biol. 2005 Dec;59(6):909-25. doi: 10.1007/s11103-005-2081-x. Plant Mol Biol. 2005. PMID: 16307366
-
Epigenetic regulation of centromere function.Cell Mol Life Sci. 2020 Aug;77(15):2899-2917. doi: 10.1007/s00018-020-03460-8. Epub 2020 Feb 1. Cell Mol Life Sci. 2020. PMID: 32008088 Free PMC article. Review.
-
Live imaging of H3K9 acetylation in plant cells.Sci Rep. 2017 Apr 18;7:45894. doi: 10.1038/srep45894. Sci Rep. 2017. PMID: 28418019 Free PMC article.
-
Centromere-specific acetylation of histone H4 in barley detected through three-dimensional microscopy.Plant Mol Biol. 2003 Mar;51(4):533-41. doi: 10.1023/a:1022375017938. Plant Mol Biol. 2003. PMID: 12650619
-
Trichostatin A and 5-azacytidine both cause an increase in global histone H4 acetylation and a decrease in global DNA and H3K9 methylation during mitosis in maize.BMC Plant Biol. 2010 Aug 18;10:178. doi: 10.1186/1471-2229-10-178. BMC Plant Biol. 2010. PMID: 20718950 Free PMC article.
References
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Research Materials