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Nuclear Pyruvate Dehydrogenase Complex regulates EIN2-directed Histone Acetylation and Transcriptional Regulation in the Ethylene Response.

ABSTRACT: Histone acetylation is important for the transcriptional regulation in the ethylene response and the nuclear metabolic production of acetyl coenzyme A (acetyl-CoA) plays key roles in histone acetylation. But how the nucleus produces acetyl-CoA for histone acetylation and transcription regulation in the ethylene response is completely unknown. Here we show that functional pyruvate dehydrogenase complex (PDC) translocates from the mitochondria to the nucleus in response to ethylene, generating nuclear acetyl CoA from pyruvate to regulate EIN2-directed histone acetylation and transcription in the target genes. It has been reported that the dephosphorylated E1 subunit of the PDC complex is required for the PDC activity, we examined the phosphorylation status change of E1 in the nucleus in response to ethylene. The MS data shows quantitative phosphorylation differences between cytosolic and nuclear fraction supporting the dephosphorylation of E1 upon ethylene treatment.

INSTRUMENT(S): Q Exactive HF

ORGANISM(S): Arabidopsis Thaliana (mouse-ear Cress)

TISSUE(S): Whole Body

SUBMITTER: Shouling Xu

LAB HEAD: Shou-Ling Xu

PROVIDER: PXD040689 | Pride | 2024-06-25

REPOSITORIES: Pride

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			Action	DRS
	Q20220706_01.pep.xml	Pepxml
	Q20220706_01.raw	Raw
	Q20220817_10.pep.xml	Pepxml
	Q20220817_10.raw	Raw
	Q20220817_14.pep.xml	Pepxml

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