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Global profiling of lysine benzoylation in S. cerevisiae

ABSTRACT: Identification of 207 Kbz sites on 149 non-histone proteins by LC-MS/MS

INSTRUMENT(S): Q Exactive

ORGANISM(S): Saccharomyces Cerevisiae (baker's Yeast)

SUBMITTER: Duo Wang

LAB HEAD: Chen Yong

PROVIDER: PXD029997 | Pride | 2022-05-20

REPOSITORIES: Pride

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			Action	DRS
	255-peptides_1_1_0.mzid.gz	Mzid
	263-peptides_1_1_0.mzid.gz	Mzid
	264-peptides_1_1_0.mzid.gz	Mzid
	QE1-298-303-peptides_1_1_0.mzid.gz	Mzid
	QE1-304-309-peptides_1_1_0.mzid.gz	Mzid

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Publications

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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HBO1 Catalyzes Lysine Benzoylation in Mammalian Cells

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LC-MS/MS identification of Kbz sites on histones catalyzed by non-enzymatic and enzymatic ways.

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Interactions between Saccharomyces cerevisiae WW domains and proteins discovered using protein microarrays

Project description:A total of 12 WW domains from Saccharomyces cerevisiae were expressed and purified as fusion proteins to either GST or MBP. The fusion proteins were chemically biotinylated and applied to duplicate protein microarrays. Data processing revealed a total of 587 interactions between the domains and 207 proteins. Most of these interactions have not been previously observed. Keywords: Protein microarray analysis of yeast WW domains

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