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Global profiling of lysine benzoylation in yeast

ABSTRACT: Proteome-wide screening of histone and non-histone Kbz sites in yeast cells

ORGANISM(S): Saccharomyces Cerevisiae

SUBMITTER: Chao Peng

PROVIDER: PXD027397 | iProX | Mon Jul 19 00:00:00 BST 2021

REPOSITORIES: iProX

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Global profiling of regulatory elements in the histone benzoylation pathway.

Wang Duo D Yan Fuxiang F Wu Ping P Ge Kexue K Li Muchun M Li Tingting T Gao Ying Y Peng Chao C Chen Yong Y

Nature communications 20220316 1

Lysine benzoylation (Kbz) is a recently discovered post-translational modification associated with active transcription. However, the proteins for maintaining and interpreting Kbz and the physiological roles of Kbz remain elusive. Here, we systematically characterize writer, eraser, and reader proteins of histone Kbz in S. cerevisiae using proteomic, biochemical, and structural approaches. Our study identifies 27 Kbz sites on yeast histones that can be regulated by cellular metabolic states. The ...[more]

PMID: 35296687

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