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Histone Modification Is Involved in Okadaic Acid (OA) Induced DNA Damage Response and G(2)-M Transition Arrest in Maize
Histone modifications are involved in regulation of chromatin structure. To investigate the relationship between chromatin modification and cell cycle regulation during plant cell proliferation, Okadaic acid (OA), a specific inhibitor of serine/threonine protein phosphatase, was applied in this stud...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2016
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4873197/ https://www.ncbi.nlm.nih.gov/pubmed/27196101 http://dx.doi.org/10.1371/journal.pone.0155852 |
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author | Zhang, Hao Wang, Pu Hou, Haoli Wen, Huan Zhou, Hong Gao, Fei Wu, Jinping Qiu, Zhengming Li, Lijia |
author_facet | Zhang, Hao Wang, Pu Hou, Haoli Wen, Huan Zhou, Hong Gao, Fei Wu, Jinping Qiu, Zhengming Li, Lijia |
author_sort | Zhang, Hao |
collection | PubMed |
description | Histone modifications are involved in regulation of chromatin structure. To investigate the relationship between chromatin modification and cell cycle regulation during plant cell proliferation, Okadaic acid (OA), a specific inhibitor of serine/threonine protein phosphatase, was applied in this study. The results showed that OA caused the cell cycle arrest at preprophase, leading to seedling growth inhibition. Western blotting assay revealed that the spatial distribution of phosphorylation of Ser10 histone H3 tails (H3S10ph) signals was altered under OA treatment. Reactive oxygen species (ROS) was found to be at higher levels and TdT-mediated dUTP nick end labeling (TUNEL) assay displayed DNA breaks happened at the chromatin after treatment with OA, companied with an increase in the acetylation of histone H4 at lysine 5 (H4K5ac) level. From these observations, we speculated that the alteration of the spatial distribution of H3S10ph and the level of H4K5ac was involved in the procedure that OA induced DNA breaks and G2-M arrested by the accumulation of ROS, and that the histone H3S10ph and H4K5ac might facilitate DNA repair by their association with the chromatin decondensation. |
format | Online Article Text |
id | pubmed-4873197 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-48731972016-06-09 Histone Modification Is Involved in Okadaic Acid (OA) Induced DNA Damage Response and G(2)-M Transition Arrest in Maize Zhang, Hao Wang, Pu Hou, Haoli Wen, Huan Zhou, Hong Gao, Fei Wu, Jinping Qiu, Zhengming Li, Lijia PLoS One Research Article Histone modifications are involved in regulation of chromatin structure. To investigate the relationship between chromatin modification and cell cycle regulation during plant cell proliferation, Okadaic acid (OA), a specific inhibitor of serine/threonine protein phosphatase, was applied in this study. The results showed that OA caused the cell cycle arrest at preprophase, leading to seedling growth inhibition. Western blotting assay revealed that the spatial distribution of phosphorylation of Ser10 histone H3 tails (H3S10ph) signals was altered under OA treatment. Reactive oxygen species (ROS) was found to be at higher levels and TdT-mediated dUTP nick end labeling (TUNEL) assay displayed DNA breaks happened at the chromatin after treatment with OA, companied with an increase in the acetylation of histone H4 at lysine 5 (H4K5ac) level. From these observations, we speculated that the alteration of the spatial distribution of H3S10ph and the level of H4K5ac was involved in the procedure that OA induced DNA breaks and G2-M arrested by the accumulation of ROS, and that the histone H3S10ph and H4K5ac might facilitate DNA repair by their association with the chromatin decondensation. Public Library of Science 2016-05-19 /pmc/articles/PMC4873197/ /pubmed/27196101 http://dx.doi.org/10.1371/journal.pone.0155852 Text en © 2016 Zhang et al http://creativecommons.org/licenses/by/4.0/ This is an open access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. |
spellingShingle | Research Article Zhang, Hao Wang, Pu Hou, Haoli Wen, Huan Zhou, Hong Gao, Fei Wu, Jinping Qiu, Zhengming Li, Lijia Histone Modification Is Involved in Okadaic Acid (OA) Induced DNA Damage Response and G(2)-M Transition Arrest in Maize |
title | Histone Modification Is Involved in Okadaic Acid (OA) Induced DNA Damage Response and G(2)-M Transition Arrest in Maize |
title_full | Histone Modification Is Involved in Okadaic Acid (OA) Induced DNA Damage Response and G(2)-M Transition Arrest in Maize |
title_fullStr | Histone Modification Is Involved in Okadaic Acid (OA) Induced DNA Damage Response and G(2)-M Transition Arrest in Maize |
title_full_unstemmed | Histone Modification Is Involved in Okadaic Acid (OA) Induced DNA Damage Response and G(2)-M Transition Arrest in Maize |
title_short | Histone Modification Is Involved in Okadaic Acid (OA) Induced DNA Damage Response and G(2)-M Transition Arrest in Maize |
title_sort | histone modification is involved in okadaic acid (oa) induced dna damage response and g(2)-m transition arrest in maize |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4873197/ https://www.ncbi.nlm.nih.gov/pubmed/27196101 http://dx.doi.org/10.1371/journal.pone.0155852 |
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