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Proteomicsc-di-GMP affect the protein acetylation through CobB dependent deacetylation
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.
ORGANISM(S): Escherichia coli 
2019-06-17 | PXD013292 | Pride
C-di-gmp cobb 
ProteomicsSILAC labeling efficiency for c-di-GMP and CobB
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, ...
ORGANISM(S): Escherichia coli 
2019-06-24 | PXD014344 | Pride
Silac c-di-gmp 
ProteomicsProtein Deacetylase CobB Interplays with c-di-GMP
As a ubiquitous bacterial secondary messenger, c-di-GMP plays key regulatory roles in processes like bacterial motility and transcription regulation. We found that c-di-GMP had impact on lysine acetylation level. To further investigate the regulation role, we performed a quantitative analysis of E. ...
ORGANISM(S): Escherichia coli 
2019-06-17 | PXD010558 | Pride
C-di-gmp Ydeh Acetylation 
UnknownInterplay between the bacterial protein deacetylase CobB and the second messenger c-di-GMP.
Not available
S-EPMC6745502 | biostudies-literature
ProteomicsIdentifing YdeH acetylation sites
we found the E. coli major DGC, YdeH, is endogenously acetylated and CobB promotes YdeH activity through deacetylation of YdeH. This experiment will identify the sites that can be acetylated by CobB on YdeH.
ORGANISM(S): Escherichia coli 
2019-06-17 | PXD008113 | Pride
Acetylation Q exactive Ydeh 
UnknownComparative Lysine Acetylome Analysis of Y. pestis YfiQ/CobB Mutants Reveals that Acetylation of SlyA Lys73 Significantly Promotes Biofilm Formation of Y. pestis.
Not available
S-EPMC10433856 | biostudies-literature
ProteomicsComprehensive profiling of lysine acetylome in Yersinia pestis
Yersinia pestis is a lethal pathogen responsible for millions of human deaths in three worldwide pandemics.The global acetylome analyses of Y. pestis grown under conditions mimicking two typical niches, i.e., the mammalian host (Mh) and the flea vector (Fv), were performed.
ORGANISM(S): Yersinia Pestis Biovar Microtus Str. 91001 
2023-07-06 | PXD038124 |
ProteomicsIdentifying protein acetylation
Five proteins, YdeH, Era, YegE, YeaJ and YihK were mixed and performed the Q Exactive MS analysis to identify the protien acetylation sites.
ORGANISM(S): Escherichia coli 
2019-06-17 | PXD007651 | Pride
Acetylation Q exactive 
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