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A small molecule defines an ecological network. Apterostigma dentigerum, a species of fungus-growing ants, utilizes Pseudonocardia actinobacteria to protect a desired species of fungus from the parasitic Escovopsis fungus. Oh et al. (p 391) use a suite of known and modified methods to first isolate the bacteria, and then isolate and characterize the small molecule that serves as an antifungal agent. The discovery of this new natural product, named dentigerumycin, will allow further studies on this interesting mutualistic community. This image shows a member of the ant colony at work in the fungal garden. Cover art by Erin Boyle, based on a photo provided by Michael Poulsen.
Understanding the structure and function of carbohydrates remains a key challenge for chemical biologists. Developments in carbohydrate synthesis and analysis together with the advent of high-throughput methods such as carbohydrate microarrays have helped shed light on the function of glycoconjugates. Similarly, consortia have provided technology platforms and focus to a burgeoning field. Now, recruitment of scientists from related fields and further integration of chemistry and biology to achieve technical goals are needed for rapid advancements.
Peptide bond formation is catalyzed from stable aminoacyl-tRNA intermediates by several specialized proteins. A new set of these enzymes forming cyclodipeptides present the first usage of tRNAs in secondary metabolism.
Efficient transport by single two-headed motor proteins requires coordination of the motor domains. A new single-molecule study sheds light on an important coordination mechanism by demonstrating an asymmetric strain dependence of the weak-to-strong binding transition in myosin-VI heads.
Synthetic agonists of sphingosine-1-phosphate receptor subtype 1 are able to generate long-term signaling that persists for hours after ligand-induced receptor internalization. These signals are independent of agonist potency, can be reversed after receptor internalization by specific antagonists, and show a distinct acyl-chain-length structure-activity relationship.
A class of proteins containing domains that are evolutionarily conserved among prokaryotes and eukaryotes was recently found to mediate post-translational AMP addition—a new protein modification called AMPylation. Similarities to the post-translational modification phosphorylation suggest that AMPylation may be an important regulatory mechanism.