Cytosolic acetyl-CoA promotes histone acetylation predominantly at H3K27 in Arabidopsis
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. (2017). Cytosolic acetyl-CoA promotes histone acetylation predominantly at H3K27 in Arabidopsis, 3(10), 814-824. http://dx.doi.org/10.1038/s41477-017-0023-7
© 2017 The Author(s). 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.
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