Abstract
Adaptive evolution by serial subcultivation of co-cultured Bacillus thuringiensis and Ketogulonicigenium vulgare significantly enhanced the productivity of 2-keto-L-gulonic acid in two-step vitamin C production. The adaptation mechanism in K. vulgare-B. thuringiensis consortium was investigated in this study based on comparative genomics and metabolomics studies. It was found that the growth, anti-oxidation, transcription and regulation were significantly enhanced in the adapted consortium. The mutation of the genes, which encode amidohydrolase in adapted K. vulgare (K150) and amino acid permease in adapted B. thuringiensis (B150), resulted in the increase of some amino acids levels in each species, and further enhanced the metabolic exchange and growth ability of the two species. Besides, the mutation of the gene encoding spore germination protein enhanced the metabolic levels of tricarboxylic acid cycle, and decreased the sporulation in B150, which induced its growth. The mutation of the genes, which encode NADPH nitroreductase in K150 and NADPH-dependent FMN reductase in B150, may enhance the ability of anti-oxidation. Overall, the long-term adaptation of K. vulgare and B. thuringiensis influenced the global regulation and made them more inseparable in metabolite exchange. Our work will provide ideas for the molecular design and optimization in microbial consortium.
Highlights
TreR yfnA BtBc_04905 BtBc_08920 BtBc_08990 BtBc_12015 azr lsrB hutH polC greA hemA BtBc_24035 mviM ftsK BtBc_26105 BtBc_27510 rho
The adaptation mechanism in K. vulgare-B. thuringiensis consortium was investigated based on comparative genomics and metabolomics studies
The amino acids exchange between K. vulgare and B. thuringiensis is so inseparable, and five mutations in B150 connect with amino acids metabolism, including amino acid permease, serine/threonine protein kinase, histone deacetylase, glutamyl-tRNA reductase and histidine ammonialyase
Summary
TreR yfnA BtBc_04905 BtBc_08920 BtBc_08990 BtBc_12015 azr lsrB hutH polC greA hemA BtBc_24035 mviM ftsK BtBc_26105 BtBc_27510 rho. NADPH nitroreductase RNA polymerase-binding protein DksA epimerase chemotaxis protein trehalose operon repressor amino acid permease MarR family transcriptional regulator hypothetical protein glycosyltransferase TetR family transcriptional regulator NADPH-dependent FMN reductase autoinducer 2-binding protein lsrB histidine ammonia-lyase PolC-type DNA polymerase III transcription elongation factor GreA glutamyl-tRNA reductase histone deacetylase virulence factor MviM cell division protein FtsK serine/threonine protein kinase glycosyl transferase transcription termination factor Rho LPXTG-domain-containing protein cell wall anchor domain glycosyl transferase family hypothetical protein hypothetical protein ribosomal protein L5 domain protein uracil-DNA glycosylase motility repressor MogR molecular chaperone Hsp[20] non-ribosomal peptide synthetase S-adenosylhomocysteine nucleosidase Lsa family ABC-F type ribosomal protection protein spore germination protein. Genetic variants of the genes that associate with metabolite modification in the key nucleosides, carbohydrates, or amino acids were studied, which enabled us to further understand the cooperative mechanism and facilitate the optimization of microbial consortium
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