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Series GSE62094 Query DataSets for GSE62094
Status Public on Oct 07, 2014
Title Lysine acetylation effect in gene expression in Escherichia coli
Platform organism Escherichia coli
Sample organism Escherichia coli K-12
Experiment type Expression profiling by array
Summary Although protein acetylation is widely observed, it has been associated with few specific regulatory functions making it poorly understood. To interrogate its functionality, we analyzed the acetylome in Escherichia coli knockout mutants of cobB, the only known sirtuin-like deacetylase, and patZ, the best-known protein acetyltransferase. For four growth conditions, more than 2,000 unique acetylated peptides, belonging to 809 proteins, were identified and differentially quantified. Nearly 65% of these proteins are related to metabolism. The global activity of CobB contributes to the deacetylation of a large number of substrates and has a major impact on physiology. Apart from the regulation of acetyl-CoA synthetase, we found that CobB-controlled acetylation of isocitrate lyase contributes to the fine-tuning of the glyoxylate shunt. Acetylation of the transcription factor RcsB prevents DNA binding, activating flagella biosynthesis and motility, and increases acid stress susceptibility. Surprisingly, deletion of patZ increased acetylation in acetate cultures, which suggests that it regulates the levels of acetylating agents. The results presented offer new insights into functional roles of protein acetylation in metabolic fitness and global cell regulation.
In this study we aimed to discover how the deregulation of protein acetylation could alter physiology in E. coli. We observed that the deletion of both cobB or patZ genes in E. coli altered gene expression, specially those genes related with motility, chemotaxis and acid stress response.
 
Overall design We used three biological replicates in this study and each condition. The control in these experiments was E. coli BW25113
 
Contributor(s) Castaño-Cerezo S, Bernal V
Citation(s) 25518064
Submission date Oct 06, 2014
Last update date Mar 08, 2019
Contact name Sara Castaño Cerezo
Organization name University of Murcia
Department Dpt. Biochemistry and Molecular Biology B and Immunology
Lab Manuel Canovas Lab
Street address Faculty of Chemistry. Campus de Espinardo. University of Murcia
City Murcia
ZIP/Postal code 30100
Country Spain
 
Platforms (1)
GPL3154 [E_coli_2] Affymetrix E. coli Genome 2.0 Array
Samples (18)
GSM1519572 E. coli wt_batch_repl1
GSM1519573 E. coli wt_batch_repl2
GSM1519574 E. coli wt_batch_repl3
Relations
BioProject PRJNA263187

Download family Format
SOFT formatted family file(s) SOFTHelp
MINiML formatted family file(s) MINiMLHelp
Series Matrix File(s) TXTHelp

Supplementary file Size Download File type/resource
GSE62094_Normalized_data_with_annotation.txt.gz 1.4 Mb (ftp)(http) TXT
GSE62094_RAW.tar 15.0 Mb (http)(custom) TAR (of CEL)
Processed data included within Sample table
Processed data are available on Series record

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