Welcome to our pick of papers and articles from last week. These are a collection of the synthetic biology papers that have captured our attention and that we think you should know about. Maybe you’ve seen some others you’d like to tell us about. Send us a comment or tweet us at @synbiobydesign. See last month’s papers here.
De novo enzyme helps E. coli survive
In this paper, the Hecht group from Princeton present a de novo enzyme, Syn-F4, which hydrolyses the siderophore ferric enterobactin. The native enzyme for this process were knocked out in E. coli to test the novel protein. Not only did it allow the E. coli to survive in the presence of ferric enterobactin, it also proved to be enantioselective, an important feature of the native enzyme. Although no crystal structure was obtained for Syn-F4, interestingly it is predicted to have a structure distinct from the enzyme it replaced. Syn-F4 joins three other de novo designed enzymes from this lab and is very exciting for potential artificial proteomes.
Establishing a transporter for modified nucleoside triphosphates
While uptake of unnatural triphosphates into cells by passive diffusion is possible, it is not always sufficient. In order to overcome the problem of importing these synthetic building blocks for RNA and DNA, Feldman et al. have expressed an algae-derived nucleoside triphosphate transporter in E. coli and developed assays to characterise its uptake.
A wholly synthetic central dogma
This perspective piece presents the arguments for a completely orthogonal DNA replication, transcription, and translation system inside a cell – much like running a virtual machine on a computer. This would solve issues of ‘compatibility’ – running a genetic program built in one host that functions optimally in a different host, and it would allow enhancements, such as increased mutagenesis rates and repurposing protein translation, to be made without detrimental effects to the host.