Proteomics identification of CsrA-regulated proteins in Legionella pneumophila

The carbon storage regulator protein CsrA regulates cellular processes post-transcriptionally by binding to target-RNAs altering translation efficiency and/or their stability. In this dataset we identified proteins regulated by CsrA in the human bacterial pathogen Legionella pneumophila by labelfree shotgun proteomics. WT and ∆csrA bacteria were grown to exponential phase in three biological replicates. Bacteria were lysed by sonication and extracted proteins were reducted, alkylated and digested with trypsin. The resulting peptide mixtures were analyzed by LC-MS/MS and proteins were identified by the MaxQuant software. In total of 1,448 proteins were quantified by the MaxLFQ algorithm in a labelfree approach. Cluster analysis showed that expression of almost all proteins was affected by the mutation of CsrA as about half of the identified proteins were up and half were down regulated. About 15% of the proteome (238 proteins) was strongly affected with 132 proteins significantly up and 109 significantly down regulated dependent on CsrA.