Project description:Purpose： The goal of this study is compare the effect of glnA gene in curdlan synthesis in Agrobacterium sp. CGMCC 11546. methods: The transcriptional and metabolomics analysis the function of glnA in Agrobacterium sp. CGMCC 11546. Results: The transcriptional and metabolomics showed that the decrease of curdlan production in the ΔglnA mutants may be caused by the insufficient supply of energy ATP conclusion: glnA play an important role in curdlan synthesis in Agrobacterium sp. CGMCC 11546
Project description:Purpose： The goal of this study is compare the effect of phbC gene in curdlan synthesis in Agrobacterium sp. CGMCC 11546. methods: The transcriptional and metabolomics analysis the function of phbC in Agrobacterium sp. CGMCC 11546. Results:The transcriptional and metabolomics showed that the decrease of curdlan production in the ΔphbC mutants may be caused by the insufficient supply of energy ATP conclusion:phbC play an important role in curdlan synthesis in Agrobacterium sp. CGMCC 11546
Project description:Purpose: The goal of this study is compare the effect of MetH and MetZ gene in curdlan synthesis in Agrobacterium sp. CGMCC 11546. methods: The transcriptional and metabolomics analysis the function of metH and metZ in Agrobacterium sp. CGMCC 11546. Results: The transcriptional and metabolomics showed that the decrease of curdlan production in the ΔmetH and ΔmetZ mutants may be caused by the insufficient supply of energy ATP conclusion: MetH and MetZ play an important role in curdlan synthesis in Agrobacterium sp. CGMCC 11546
Project description:We report the analysis of differentially gene expression after 7 hours and 24 hours fermentation of curdlan in Agrobacterium sp. CGMCC 11546.
Project description:Proteomic Analysis. The proteomic expression of CGMCC 6315 under different nutrient concentration conditions was investigated by isobaric tags for relative and absolute quantitation (iTRAQ)-based quantitative proteomics. The CGMCC 6315 was cultured in LB broth and 1/15LB broth as described above, after which the strains were collected by centrifugation at 10,000× g for 10 min at 4°C. Protein extraction, digestion, iTRAQ labeling and peptide fractionation were performed using the protocol described by Jin et al. 29. Protein identification was conducted using a LC-20AD nano-HPLC instrument (Shimadzu, Kyoto, Japan) equipped with a Q EXACTIVE tandem mass spectrometer (Thermo Fisher Scientific, San Jose, CA, USA) for data-dependent acquisition detection by nano-electrospray ionization. The raw MS/MS data were converted into MGF format by the thermo scientific tool Proteome Discoverer, and the exported MGF files were searched using Mascot (version 2.3.02) against the selected database containing 7546 CGMCC 6315 coding genes. The IQuant software was used for quantitative analysis of the labeled peptides with isobaric tags. Fold changes of >1.7 with p-values <0.05 were used as a cut off for differentially regulated proteins.
Project description:We conducted transcriptome analysis of Komagataeibacter europaeus CGMCC 20445 samples under different acidity conditions to elucidate the changes in differentially expressed genes throughout the fermentation process.
Project description:Mycobacterium marinum is a pathogenic bacterium that causes infections in both fish and humans. The PE/PPE protein family is unique to mycobacteria and has been implicated in various aspects of mycobacterial pathogenicity. Understanding the presence and potential function of these proteins in M. marinum is essential for unraveling the mechanisms underlying its virulence. In this study, we conducted a proteomics analysis to investigate the secretion and potential role of the PE/PPE protein family in the culture filtrate of M. marinum. To investigate the presence of PE/PPE proteins in the culture filtrate, we employed a proteomics approach combining Asp-N and trypsin based digestion. Cultures of M. marinum were grown under laboratory conditions, and the culture filtrate was collected and subjected to digestion and LC-MS injection. Our proteomics analysis revealed the secretion of about half PE/PPE proteins in the culture filtrate of M. marinum. Majority of these proteins are confirmed to be involved in EspG5 interaction. The identification of these proteins in the culture filtrate suggests their secretion and potential role in M. marinum. Our proteomics analysis highlights the presence of PE/PPE proteins in the culture filtrate of M. marinum, suggesting their secretion and potential involvement in the pathogenicity of this bacterium.
