Thank you for visiting nature.com. You are using a browser version with limited support for CSS. To obtain
the best experience, we recommend you use a more up to date browser (or turn off compatibility mode in
Internet Explorer). In the meantime, to ensure continued support, we are displaying the site without styles
and JavaScript.
Since the 1980s, scientists have worked on designing genetic codes to reinforce containment and control of genetically engineered microbes. New mechanistic studies of “deadman” and “passcode” gene circuits provide a flexible platform to build new safety switches.
Protein aggregation is associated with more than 50 human pathologies, including prevalent conditions such as Alzheimer's and Parkinson's diseases. A phenotypic screen in Escherichia coli associating antibiotic resistance with the inhibition of protein aggregation now allows screening for chemical inhibitors of protein aggregation in a simple, fast and inexpensive manner.
A small molecule's biological activity in a cell depends on the actions of many gene products. Correlations between basal gene expression and compound sensitivity across hundreds of human cell lines reveal a broad view of cellular mechanisms of action.
This Perspective discusses recent advances in understanding the biochemistry, enzymology and cell biology of Wnt fatty acylation and its effects on signaling and cancer.
Expansion of the genetic code to noncanonical amino acids (NCAAs) has been limited by the lack of evolutionary pressure for organismal dependence on the NCAA. Linking bacterial survival to an engineered β-lactamase that requires a non-natural tyrosine analog engenders diverse bacteria with a stable, expanded genetic code.
A scan of the protein structure database looking for interhelical contacts across transmembrane protein helix trimers finds six distinct structural and topological classes with unique sequence-3D contact motifs that could prove useful in future protein design initiatives.
The antifungal drug naftifine blocks carotenoid pigment biosynthesis in Staphylococcus aureus through inhibition of a biosynthetic enzyme of staphyloxanthin, disabling an important virulence mechanism and thus making the pathogen susceptible to host oxidant killing.
The protonation state of Glu14 within the drug transporter EmrE is able to influence the conformational dynamics of the protein and thereby bias the inward-open conformation to facilitate substrate efflux.
Oscillations of actin, FBP17 and N-WASP are coupled to phase-shifted phosphoinositide (PI) turnover that is regulated by the lipid phosphatases SHIP1, synaptojanin 2 and PI 3-kinases. PI(4,5)P2 turnover regulates wave amplitude and PI(3,4)P2 acts as a pacemaker.
XSI analysis of two RNA kink-turn motifs, KtA and KtB, in a range of solution concentrations and in the presence of the kink-turn protein partner L7Ae reveals a restricted conformational ensemble that is regulated by ions and protein binding.
Point mutations in nascent peptides that regulate in the macrolide antibiotic resistance genes ermC and ermB can tune the recognition of the antibiotics erythromycin and telithromycin that control ribosome stalling and gene activation.