https://scholars.lib.ntu.edu.tw/handle/123456789/414212
Title: | Cytosolic acetyl-CoA promotes histone acetylation predominantly at H3K27 in Arabidopsis | Authors: | Chen C. Li C. Wang Y. Renaud J. Tian G. Kambhampati S. Saatian B. Nguyen V. Hannoufa A. Marsolais F. Yuan Z.-C. Yu K. Austin R.S. Liu J. Kohalmi S.E. Wu K. Huang S. Cui Y. |
Issue Date: | 2017 | Journal Volume: | 3 | Journal Issue: | 10 | Start page/Pages: | 814-824 | Source: | Nature Plants | Abstract: | Acetyl-coenzyme A (acetyl-CoA) is a central metabolite and the acetyl source for protein acetylation, particularly histone acetylation that promotes gene expression. However, the effect of acetyl-CoA levels on histone acetylation status in plants remains unknown. Here, we show that malfunctioned cytosolic acetyl-CoA carboxylase1 (ACC1) in Arabidopsis leads to elevated levels of acetyl-CoA and promotes histone hyperacetylation predominantly at lysine 27 of histone H3 (H3K27). The increase of H3K27 acetylation (H3K27ac) is dependent on adenosine triphosphate (ATP)-citrate lyase which cleaves citrate to acetyl-CoA in the cytoplasm, and requires histone acetyltransferase GCN5. A comprehensive analysis of the transcriptome and metabolome in combination with the genome-wide H3K27ac profiles of acc1 mutants demonstrate the dynamic changes in H3K27ac, gene transcripts and metabolites occurring in the cell by the increased levels of acetyl-CoA. This study suggests that H3K27ac is an important link between cytosolic acetyl-CoA level and gene expression in response to the dynamic metabolic environments in plants. ? 2017 The Author(s). |
URI: | https://scholars.lib.ntu.edu.tw/handle/123456789/414212 | ISSN: | 20550278 | DOI: | 10.1038/s41477-017-0023-7 |
Appears in Collections: | 植物科學研究所 |
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