Title : Cytosolic acetyl-CoA promotes histone acetylation predominantly at H3K27 in Arabidopsis.

Pub. Date : 2017 Oct

PMID : 28947800






4 Functional Relationships(s)
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1 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). Acetyl Coenzyme A acetyl-CoA carboxylase 1 Arabidopsis thaliana
2 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). Lysine acetyl-CoA carboxylase 1 Arabidopsis thaliana
3 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). Lysine acetyl-CoA carboxylase 1 Arabidopsis thaliana
4 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. Acetyl Coenzyme A acetyl-CoA carboxylase 1 Arabidopsis thaliana