Proteomics

Dataset Information

0

SILAC labeling efficiency for c-di-GMP and CobB


ABSTRACT: Description 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. Before that, we determined the labeling efficiency for these samples.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Escherichia Coli

SUBMITTER: Zhaowei Xu  

LAB HEAD: Zhaowei Xu

PROVIDER: PXD014344 | Pride | 2019-06-24

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
20190321_Ecoli_heavy.raw Raw
20190321_Ecoli_heavy.xlsx Xlsx
20190321_Ecoli_medium.raw Raw
20190321_Ecoli_medium.xlsx Xlsx
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Publications


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]

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