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Histone lysine acetylation, butyrylation, and crotonylation dynamics and functional interplay in rice under starvation and submergence

ABSTRACT: Histone lysine acylations are regulated by primary metabolism in animal cells. However, histone non-acetyl acylation is not yet studied in plants that have distinct primary metabolic pathways. In this work, we detected rice histone lysine butyrylation (Kbu) and crotonylation (Kcr) sites by mass spectrometry, and found both similar and specific acylation patterns compared with that in mammalian cells.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Oryza Sativa (rice)

TISSUE(S): Leaf

SUBMITTER: qiutao xu

LAB HEAD: Dao-Xiu Zhou

PROVIDER: PXD009091 | Pride | 2018-09-06

REPOSITORIES: Pride

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Dynamics and functional interplay of histone lysine butyrylation, crotonylation, and acetylation in rice under starvation and submergence.

Lu Yue Y Xu Qiutao Q Liu Yuan Y Yu Yue Y Cheng Zhong-Yi ZY Zhao Yu Y Zhou Dao-Xiu DX

Genome biology 20180925 1

<h4>Background</h4>Histone lysine acylations by short-chain fatty acids are distinct from the widely studied histone lysine acetylation in chromatin, although both modifications are regulated by primary metabolism in mammalian cells. It remains unknown whether and how histone acylation and acetylation interact to regulate gene expression in plants that have distinct regulatory pathways of primary metabolism.<h4>Results</h4>We identify 4 lysine butyrylation (Kbu) sites (H3K14, H4K12, H2BK42, and ...[more]

PMID: 30253806

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Global involvement of lysine crotonylation in protein modification and transcription regulation in rice

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