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Widespread protein histidine phosphorylation in bacteria

ABSTRACT: For decades, extreme difficulties in analyzing histidine phosphorylation have limited the study of phosphohistidine signaling. Here we report a method revealing widespread and abundant protein histidine phosphorylation in E. coli. Our new approach generated the largest E. coli phosphoproteome dataset to date, of which a remarkable high percentage (~10%) are phosphohistidine sites. This resource enables a major step forward towards a better understanding of the biological function of histidine phosphorylation.

ORGANISM(S): Escherichia Coli

SUBMITTER: Albert J.R. Heck

PROVIDER: PXD008369 | JPOST Repository | Thu Dec 07 00:00:00 GMT 2017

REPOSITORIES: jPOST

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			Action	DRS
	Ecoli_phospho_txt_glycerol_glucose_optimized.zip	Other
	OR10_20160316_CMP_Ecoli_glucose_exp_4mg_IMAC_80pc.raw	Raw
	OR10_20160316_CMP_Ecoli_glucose_stat_4mg_IMAC_80pc.raw	Raw
	OR10_20160316_CMP_Ecoli_glyc_stat_4mg_IMAC_80pc.raw	Raw
	OR11_20160131_CMP_Ecoli_1mg_IMAC_80pc.raw	Raw

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Widespread bacterial protein histidine phosphorylation revealed by mass spectrometry-based proteomics.

Potel Clement M CM Lin Miao-Hsia MH Heck Albert J R AJR Lemeer Simone S

Nature methods 20180129 3

For decades, major difficulties in analyzing histidine phosphorylation have limited the study of phosphohistidine signaling. Here we report a method revealing widespread and abundant protein histidine phosphorylation in Escherichia coli. We generated an extensive E. coli phosphoproteome data set, in which a remarkably high percentage (∼10%) of phosphorylation sites are phosphohistidine sites. This resource should help enable a better understanding of the biological function of histidine phosphor ...[more]

PMID: 29377012

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