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Using single-molecule fluorescence resonance energy transfer (smFRET), Kim et al. (p 763) demonstrate that the 8-17 DNAzyme, one of the newest members of the metalloenzyme family, uses both induced fit and lock-and-key modes of catalysis, much like its proteinaceous relatives (see also News and Views by Schlosser and Li, p 753). Shown is an smFRET image beneath a schematic representation of DNAzyme catalysis, with the 8-17 DNAzyme strand in blue and the substrate in red(labeled with a FRET donor in yellow and acceptor in orange). The path on the left demonstrates global folding that occurs prior to cleavage and release of the product. The path on the right depicts binding to a prearranged DNA structure. Cover art by Erin Boyle, based on imagery provided by Alex D. Jerez, Hee-Kyung Kim and Yi Lu.
Education is a central mission of universities. Emphasizing creative and passionate teaching by all academic staff is essential for maintaining educational quality while supporting vigorous research.
The biology of RNA interference has greatly facilitated analysis of loss-of-function phenotypes, but correlating these phenotypes with small-molecule inhibition profiles is not always straightforward. We examine the rationale of comparing RNA interference to pharmacological intervention in chemical biology.
DNA is the newest member of the enzyme club. The first glimpse of DNAzyme conformational changes at the single-molecule level reveals that enzymes made of DNA can use the same modi operandi as protein and RNA catalysts.
Pharmacological and genetic modulators of voltage-gated Ca2+ channel (CaV) activity have been useful tools for understanding and modulating excitable cell function. A new method combines these approaches to provide pharmacological control of a genetically encoded suppressor of CaV activity.
Multimodular scaffold proteins are ideally suited for assembling the various proteins in signaling pathways into supramolecular complexes. A recent study demonstrates that, in addition to a passive scaffolding role, a PDZ domain in a photoreceptor scaffold protein actively regulates fruit fly visual signaling via light-dependent conformational cycling.