Researchers studied 36 DNA-based molecular junctions and discovered factors that yield superior self-assembled 3D lattice structures. The work expands the set of building blocks for lattices that can scaffold molecules into regular arrays, from proteins for structure studies to nanoparticles for nano-antennas and single-particle sensors. Read more »
Protein Structures Aren’t Set in Stone
A group of researchers studying the world’s most abundant protein, an enzyme involved in photosynthesis called rubisco, showed how evolution can lead to a surprising diversity of molecular assemblies that all accomplish the same task. The findings reveal the possibility that many of the proteins we thought we knew actually exist in other, unknown shapes. Read more »
Deep-Learning AI Program Accurately Predicts Key Rotavirus Protein Fold
Rotaviruses are the major causative agents of gastroenteritis worldwide. Attempts to design vaccines are complicated by the rotaviruses’ enormous genetic and immunological diversity. At the ALS, researchers validated the novel structure of a key rotavirus protein, predicted using AlphaFold2, a deep-learning artificial-intelligence program. Read more »
Molecular Switch Triggers Changes in Plant Structure
Using x-ray crystallography, biochemistry, and plant genetics, researchers identified a molecular switch that triggers modifications to plant structure in response to environmental conditions. A greater understanding of this adaptive process will help scientists optimize plants for efficient nutrient uptake and resistance to parasitic species. Read more »
Phosphomimetic S207D Lysyl–tRNA Synthetase Binds HIV-1 5′UTR in an Open Conformation and Increases RNA Dynamics
Binding assays, RNA chemical probing, and SAXS showed that phosphomimetic S207D LysRS binds in an open conformation preferentially to dimeric HIV-1 genomic RNA. A new working model is proposed wherein a dimeric phosphorylated LysRS/tRNA complex binds to a genomic RNA dimer, facilitating tRNA primer release and placement onto the binding site. Future anti-viral strategies that prevent this interaction are envisioned. Read more »
Bacterial Enzyme Produces Biodegradable Polymer
Researchers discovered a bacterial enzyme that synthesizes a biopolymer whose repeating units are linked together in way that had not been previously observed. The new polymer is biodegradable and may be biocompatible, with potential for applications ranging from medical therapeutics to eco-friendly plastic alternatives. Read more »
Newly Discovered Bacterial Enzyme Produces Useful Biopolymer
Researchers identified a bacterial enzyme that produces a novel biopolymer. The polymer, dubbed acholetin, is a chain of sugar molecules known as a polysaccharide. Acholetin is similar in structure to chitin, the major component of insect exoskeletons, and holds promise as a useful biomaterial because of its biodegradability and biocompatibility. Read more »
Molecular Hijacking of a MicroRNA by the Hepatitis C Virus
The hepatitis C virus (HCV), which attacks the liver, is known to repurpose host-cell components known as microRNAs—short RNA strands that act to silence gene expression. Now, the molecular structure of an HCV site bound to a microRNA complex revealed how their interactions shield the virus from the host cell’s protective response. Read more »
Biomineralization: Integrating mechanism and evolutionary history
In this review, Gilbert et al. develop a model for calcium carbonate biomineralization applicable to all phyla. Their model may help elucidate the key genetic components that drive biomineralization and offers insight into the consequences of global climate change on marine organisms. Read more »
Loss of biological control of enamel mineralization in amelogenin-phosphorylation-deficient mice
Amelogenin phosphorylation plays crucial roles in controlling structural, crystallographic, mechanical, and compositional characteristics of dental enamel. Thus, loss of amelogenin phosphorylation leads to a reduction in the biological control over the enamel mineralization process. Read more »
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