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Dewald, J. A.

Publications and source records attributed to Dewald, J. A..

2 recordsLinked to original sources

When a chaotropic agent turns into a nutrient: Deciphering the assimilation of guanidine and its utilization to drive synthetic processes in cyanobacteria

Guanidine is a well-known chaotropic agent used to denature proteins and nucleic acids. However, recent studies have demonstrated both the widespread synthesis of guanidine, e.g. in plants and mammals, as well as the widespread occurrence of guanidine metabolism in bacteria, suggesting a broader biological role. Here, we provide insights into guanidine assimilation via guanidine hydrolases (GdmH) in cyanobacteria. The gdmH gene is widespread among cyanobacteria and enables growth on guanidine as sole nitrogen source. Strains lacking gdmH, naturally or by deletion, failed to grow on guanidine. Expression of gdmH increased under nitrogen limitation, regulated by the transcription factor NtcA. However, guanidine is toxic above 5 mM, necessitating GdmH activity and adaptive mutations activating the multidrug efflux system PrqA. The gdmH gene is frequently co-localized with ABC transporter genes, which are driven by an additional NtcA-regulated promoter. At low guanidine concentrations, their mutation disrupted guanidine-dependent growth of Synechocystis sp. PCC 6803, supporting that they encode a high affinity transport system. In presence of >1 mM guanidine, these mutants grew like wildtype, suggesting the existence of additional uptake mechanisms for guanidine. We next demonstrate the high-affinity binding of guanidine to a previously described, conserved RNA motif located within the gdmH 5 UTR, validating it as a guanidine I riboswitch. By combining it with various promoters, we achieved precise, titratable control of heterologous gene expression in cyanobacteria in vivo. Our findings establish guanidine assimilation as an integral element of cyanobacterial nitrogen metabolism and highlight guanidine riboswitches as valuable tools for synthetic biology. Significance statementCyanobacteria are promising whole-cell biocatalysts for the sustainable, CO2-neutral production of chemicals and fuels. Unlocking this potential requires deep understanding of their metabolism and advanced molecular tools for genetic engineering. We show that cyanobacteria can assimilate guanidine as sole nitrogen source. Because of its toxicity, guanidine metabolism is tightly controlled, involving the transcription factor NtcA and a riboswitch, an RNA element regulating gene expression by guanidine binding. By utilizing this riboswitch, we achieved precise regulation of heterologous genes. Guanidine is inexpensive and effective at low concentrations, making large-scale applications in cyanobacterial cell factories cost-efficient. This study advances our understanding of the metabolic capacities of environmentally important cyanobacteria and their metabolic engineering, highlighting riboswitches as valuable tools for controlling biotechnological processes.

microbiology↗

Ancient origin and high diversity of zymocin-like killer toxins in the budding yeast subphylum

Zymocin is a well-characterized killer toxin secreted by some strains of the yeast Kluyveromyces lactis. It acts by cleaving a specific tRNA in sensitive recipient cells. Zymocin is encoded by a killer plasmid or virus-like element (VLE), which is a linear DNA molecule located in the cytosol. We hypothesized that a tRNA-cleaving toxin similar to zymocin may have caused the three parallel changes to the nuclear genetic code that occurred during yeast evolution, in which the codon CUG became translated as Ser or Ala instead of Leu. However, zymocin-like toxins are rare - both among species, and among strains within a species - and only four toxins of this type have previously been discovered. Here, we identified 45 new zymocin-like toxin genes in Saccharomycotina, the budding yeast subphylum, using a novel bioinformatics strategy, and verified that many of them are toxic to S. cerevisiae when expressed. Some of the new toxin genes are located on cytosolic VLEs, whereas others are on VLE-derived DNA integrated into the nuclear genome. The toxins are extraordinarily diverse in sequence and show evidence of positive selection. Toxin genes were found in five taxonomic orders of budding yeasts, including two of the three orders that reassigned CUG codons, indicating that VLEs have been parasites of yeast species for at least 300 million years and that their existence pre-dates the genetic code changes.

evolutionary biology↗