Project description:We report the application of transcriptome sequencing technology for high-throughput profiling of Serratia marcescens for producing prodigiosin. By obtaining over 163 million bases of sequence from Serratia marcescens genome DNA, we generated transcriptome -state maps of Serratia marcescens 12h cells, 24h cells, and 36h cells at 30C and 37C,respectively. We explored the mechanism of S. marcescens response temperature regulation at the transcription level through transcriptome sequencing technology. We found that the pig gene cluster at low temperature would favor at the transcriptional level, however, higher temperature resulting in instability and loss of enzyme activity. Numerous amino acid metabolic pathways involved in prodigiosin biosynthesis in S. marcescens responded to temperature changes, and metabolic fluxes were directed towards prodigiosin biosynthesis. At the same time, quorum sensing, two-component regulatory system and sRNA were stimulated by temperature to regulate PG biosynthesis and involve strain virulence and exclusive genes. Moreover, inhibition factors was the one reason for S. marcescens incapable synthesis of prodigiosin at 37C. This study laid a good foundation for understanding the biological functions of prodigiosin, improving the temperature tolerance of industrial strains, and excavating temperature-sensitive regulatory elements.
Project description:The EepR protein is a two-component response regulator protein in the bacterium Serratia marcescens. Mutation of the eepR gene results in pleiotropic changes including reduced expression of secondary metabolites and proteases.
Project description:Serratia marcescens (S. marcescens), an opportunistic human pathogen, has been identified as a major cause of nosocomial infection and outbreaks. The purpose of this analysis is to examine the S. marcescens (ATCC 13880) protein profile using a high resolution mass spectrometry (MS). S. marcescens ATCC 13880 strain was grown in Luria-Bertani broth and the protein extracted underwent trypsin digestion followed by simple reverse phase liquid chromatography fractionation. Peptide fractions were then analyzed using Orbitrap Fusion Mass Spectrometry and raw MS data was processed using Proteome Discoverer software. The proteomic study identified 2,541 unique protein groups, corresponding to approximately 54% of the measured protein-coding genes. Bioinformatics analysis of these identified proteins demonstrated their involvement in biological processes such as cell wall organization, caperone-mediated protein folding and ATP binding. To our knowledge, this is the first high-performance S.marcescens proteomics analysis (ATCC 13880). These novel observations provide a key baseline molecular profile of the S. marcescens proteome which will prove to be helpful for the future research in understanding the host-pathogen interactions during infection, elucidating the mechanism of multidrug resistance and for developing novel diagnostic markers or vaccine for the disease.