Dataset Information

C-di-GMP affect the protein acetylation through CobB dependent deacetylation

ABSTRACT: To determine whether c-di-GMP could affect CobB-dependent deacetylation in a global setting, we applied Stable Isotope Labeling with Amino acids in Cell culture (SILAC) coupled with MS to quantitatively compare the levels of protein acetylation in WT, ΔcobB and ΔdgcZ cells.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Escherichia Coli

SUBMITTER: Zhaowei Xu

LAB HEAD: Shengce Tao

PROVIDER: PXD013292 | Pride | 2019-06-17

REPOSITORIES: pride

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Dataset's files

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			Action	DRS
	20190228_Ecoli_acetylation_IP_1.raw	Raw
	20190228_Ecoli_acetylation_IP_1.xml	Xml
	20190321_ECOLI_2.raw	Raw
	20190321_ECOLI_2.xml	Xml
	20190326_Ecoli_acetylation_IP_2.raw	Raw

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Publications

Interplay between the bacterial protein deacetylase CobB and the second messenger c-di-GMP.

Xu Zhaowei Z Zhang Hainan H Zhang Xingrun X Jiang Hewei H Liu Chengxi C Wu Fanlin F Qian Lili L Hao Bingbing B Czajkowsky Daniel M DM Guo Shujuan S Xu Zhijing Z Bi Lijun L Wang Shihua S Li Haitao H Tan Minjia M Yan Wei W Feng Lei L Hou Jingli J Tao Sheng-Ce SC

The EMBO journal 20190816 18

As a ubiquitous bacterial secondary messenger, c-di-GMP plays key regulatory roles in processes such as bacterial motility and transcription regulation. CobB is the Sir2 family protein deacetylase that controls energy metabolism, chemotaxis, and DNA supercoiling in many bacteria. Using an Escherichia coli proteome microarray, we found that c-di-GMP strongly binds to CobB. Further, protein deacetylation assays showed that c-di-GMP inhibits the activity of CobB and thereby modulates the biogenesis ...[more]

PMID: 31418899

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