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Scientific Highlights

RNA molecules, often bound to protein in complexes, play essential roles in many basic cellular processes in all life. Like with proteins, often these roles depend on the distinct 3-dimensional shapes the RNA molecules adopt. While much research has been done using traditional biophysical techniques to determine the predominant structure of many RNA folds, less is known about the array of shapes a certain type of RNA can adopt and how this ensemble of form affects function.
Many organisms produce chemicals known as secondary metabolites that are not directly vital for survival but often play important roles in the organisms’ defense against other species. Due to their wide range of medically relevant properties, these compounds are also of great interest to humankind. The secondary metabolite erythromycin, for instance, is an important antibiotic of bacterial origin. Recently, researchers have shed light on the structural architecture of 6-deoxyerythronolide B synthase (DEBS) – a large multi-protein complex that acts as an assembly line for one of erythromycin’s precursors.
Aminoacyl-tRNA synthetases are required in all three domains of life to add the correct amino acid to its cognate tRNA, an essential step in protein synthesis. Despite their importance, no structure had been reported for any full-length eukaryotic, glutaminyl-tRNA synthetase (GlnRS), although structural data for two prokaryotic GlnRS species exists.
Of the 11 species of Neisseria bacteria that colonize humans, 9 of them coexist peacefully with us. However, two can cause serious diseases N. gonorrhoeae, responsible for the sexually transmitted disease gonorrhea, and N. meningitidis, which causes septicemia and meningitis. Commercially available vaccines exist for four of the five known disease-causing serogroups of N. meningitidis (A, B, C, Y, W135) but no vaccine exists to combat serogroup B (menB); nor is there a vaccine available against N. gonorrhoeae. One target for vaccine development against menB and N. gonorrhoeae is the iron transporters found on the pathogens’ surfaces. Cut off their access to iron and these pathogens cannot survive.
Programmed cell death, or apoptosis, is a critical failsafe against uncontrolled proliferation. For this reason, apoptosis is frequently defective in cancer cells, allowing tumor growth to proceed unchecked. The inhibitor of apoptosis proteins, or IAPs, are some of the final “brakes” on apoptosis, directly inhibiting both caspases and their upstream activators (1,2,3,4). Thus it is unsurprising that IAP proteins are over-expressed in many human cancers (2,5).