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.2019-07-172019-07-17201720550278https://scholars.lib.ntu.edu.tw/handle/123456789/414212Acetyl-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).[SDGs]SDG3journal article10.1038/s41477-017-0023-72-s2.0-85029781529https://www.scopus.com/inward/record.uri?eid=2-s2.0-85029781529&doi=10.1038%2fs41477-017-0023-7&partnerID=40&md5=7c2df3cd6fd35877e653045cee11e4e9