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:Lariat RNAs, generated as by-products of RNA splicing from excised introns, must be removed. RNA debranching enzyme (DBR1) is the core factor responsible for lariat RNA removal. However, the mechanism by which DBR1 debranches lariat RNAs remains unclear. Here, we demonstrate that six ALBA (Acetylation Lowers Binding Affinity) proteins interact with DBR1 to enhance its debranching activity and facilitate DBR1's accessibility to lariat RNAs, thereby promoting lariat RNA turnover. Similar to dbr1, alba mutants exhibit pleiotropic developmental defects and accumulate lariat RNAs. ALBAs bind to lariat RNAs via their C-terminal RGG/RG-rich repeats and assist DBR1 in binding to these RNAs. The N-terminal ALBA domain mediates the interaction with DBR1 and enhances its enzymatic activity. Cold stress induces lariat RNA accumulation by attenuating the ALBA–DBR1 interaction, which in turn reduces the induction of cold-responsive genes by impairing their transcription. Together, these findings uncover that lariat RNA turnover requires ALBA proteins.
