Mutant of AroG and application of mutant in amino acid producing genetically engineered bacteria
A genetically engineered bacteria, genetic engineering technology, applied in bacteria, microorganism-based methods, enzymes, etc., can solve problems such as difficulty in confirming impact, expensive raw materials, and complex processes
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Embodiment 1
[0026] Embodiment 1, construction bacterial strain BDZ1
[0027] The wild-type genes involved in this example and their accession numbers in GenBank are: ID of aroG: 945605, ID of rpoS: 947210, ID of ppsA: 946209, ID of trpR: 948917, ID of tnaA: 948221.
[0028] Construction of PH5a-aroG-trpEDCBA plasmid: Using wild-type Escherichia coli MG1655 as a template, the aroG fragment with linker was amplified with primers aroG-F and aroG-R. Using the PH5a plasmid as a template, PH5a-M-F and PH5a-M-R amplify the PH5a-M fragment with a linker. Using the aroG fragment and the PH5a-M fragment as templates, the aroG-F and PH5a-M-R primers were amplified to obtain the aroG-M-Gibson fragment for Gibson assembly. Using MG1655 as a template, primers trpEDCBA-F and trpEDCBA-R were used to amplify the trpEDCBA-Gibson fragment with adapter. Use PH5a-ver-F and PH5a-ver-R to amplify the plasmid backbone with adapters, and use the above aroG-M-Gibson fragment and trpEDCBA-Gibson fragment to obtai...
Embodiment 2
[0039] Embodiment 2, construction bacterial strain BDZ2
[0040] DAHP synthase AroG catalyzes the formation of DAHP from two important precursors, phosphoenolpyruvate (PEP) and erythrose-4-phosphate (E4P), thereby entering the shikimate pathway. AroG occupies a key site in the tryptophan synthesis pathway, but AroG is subject to feedback inhibition by L-phenylalanine, so releasing the inhibitory effect of phenylalanine on AroG is critical to expanding the metabolic flux of the shikimate pathway. Aiming at the inhibitory effect of L-phenylalanine on AroG, after docking of L-phenylalanine and AroG protein (PDB: 5CKS), it was found that the 180th amino acid (S) and the 6th amino acid in the AroG protein (Q) directly formed a hydrogen bond interaction with L-phenylalanine. In order to relieve the inhibitory effect of phenylalanine, the S211 residue of AroG was replaced by F, and the benzene ring in the mutated F directly occupied part of the binding position of the inhibitor L-ph...
Embodiment 3
[0049] Example 3, construction of L-tryptophan production strain BDZ3
[0050] RpoS code σ s , is a subunit of RNA polymerase that acts as a master regulator of the adaptation of many stationary-phase genes to nutrient deprivation and other stresses in Escherichia coli. Genome-wide analysis of RpoS-dependent gene expression revealed that up to 10% of genes in E. coli are directly or indirectly regulated by RpoS. Although the RpoS regulator is a huge conserved system that is essential for adaptation to various stressful stresses, its regulatory mechanism in specific metabolic pathways, such as the L-tryptophan synthesis pathway, is still not fully understood. Therefore, the present invention introduces the mutation site Q33* to inactivate RpoS, thereby determining the influence of RpoS on the L-tryptophan synthesis pathway.
[0051] Cas9-rpoS plasmid construction: use MG1655 as template, use primers rpoS-up-F, rpoS-up-R to amplify the rpoS-up fragment with linker, and use pri...
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