Structural biology has elucidated the mechanism of a configuration-specific enzyme that decouples D-amino acids from the translational machinery and, therefore, is involved in the enforcement of homochirality during protein synthesis.
The first genomic view of beetle luciferase evolution indicates evolutionary independence of luciferase between fireflies and click-beetles, and provide valuable datasets which will accelerate the discovery of new biotechnological tools.
Human cullin-RING ligases are buffered to a much greater extent than had been previously appreciated, and the roles of ubiquitin chain extension enzymes are far more nuanced at physiological concentrations.
In fruit flies, maternally deposited RNA-binding proteins are removed during the maternal-to-zygotic transition via a mechanism of translational upregulation of Kondo, the key E2 enzyme, at egg activation.
Crosslinking the AAA+ protease interface does not abolish protein degradation by ClpAP, establishing that rotation of the AAA+ unfoldase with respect to its partner peptidase is not essential for activity.
The first structure of a bacteriophage-encoded S-adenosyl methionine degrading enzyme was solved and demonstrated to catalyze a unimolecular lyase reaction occurring at the domain interface of a trimeric structure.