An enzyme as key to protein quality
Peer-Reviewed Publication
Updates every hour. Last Updated: 26-Jun-2025 13:10 ET (26-Jun-2025 17:10 GMT/UTC)
In neurodegenerative diseases such as Alzheimer's or Parkinson's, proteins accumulate in the body's cells, fold incorrectly and clump together to form larger aggregates. Normally, cells are able to remove these aggregates themselves. However, if a certain enzyme is blocked, this clean-up process no longer works. This is shown in a new study by an international research team led by the University of Würzburg. The new findings provide a better understanding of the molecular basis of these processes.
Researchers from A*STAR Institute of Molecular and Cell Biology (A*STAR IMCB) and local biotechnology company Intra-ImmuSG have announced promising outcomes from a Phase II clinical trial of a novel cancer immunotherapy, PRL3-zumab. Published in Cell Reports Medicine, the study shows PRL3-zumab safely slows disease progression in patients with advanced solid cancers unresponsive to existing treatments.
The North Korean government engages in unsustainable and illegal wildlife trade, which includes species protected under its own laws and poses a threat to biodiversity recovery in the region, finds a groundbreaking new study by UCL researchers.
Some plants lure pollinators not with sweet fragrances, but with the rank stench of decay. In a new study, researchers show how plants pull this off. In Asarum flowers, a gene typically used for detoxifying smelly compounds has instead evolved to produce unpleasant odors, the researchers report. The findings shed light on how plants co-opt widely conserved metabolic pathways for ecological advantage. A key feature of foul-smelling flowers is the release of malodorous volatile compounds, particularly oligosulfides like dimethyl disulfide (DMDS) and dimethyl trisulfide (DMTS). These compounds mimic the chemical signals given off by decaying material. While it's known that these compounds originate from the bacterial breakdown of sulfur-containing amino acids, the biological mechanisms that allow flowers to produce them remain largely unknown. To explore this, Yudai Okuyama studied flowers from the Asarum genus, which display remarkable diversity in form and scent – traits believed to have evolved to lure a wide range of insect pollinators.
Through comparative genomics and functional assays, Okuyama et al. discovered that the floral emission of DMDS is linked to the expression of a gene from the selenium-binding protein family. In humans, the related protein, SELENBP1, typically detoxifies methanethiol – a compound with a strong, smelly odor that underlies clinical bad breath. It detoxifies methanethiol by converting it into less harmful substances. In Asarum species, Okuyama et al. found three distinct types of methanethiol oxidase genes—SBP1, SBP2, and SBP3. By expressing these genes in bacteria and testing their enzymatic function, they found that SBP1 performs a unique reaction: instead of detoxifying methanethiol, it transforms it into DMDS. This ability arose through a small number of amino acid changes in SBP1, which switched SBP1’s enzyme function from a methanethiol oxidase (MTOX) to a disulfide synthase (DSS). This appears to have evolved independently in at least three unrelated plant lineages, pointing to convergent evolution driven by similar ecological pressures. “It is notable that although methanethiol oxidation, the ancestral enzymatic activity, is also observed in humans, enzymatic oligosulfide synthase activity has only evolved in plants,” write Lorenzo Caputi and Sarah O’Conner in a related Perspective. “This is likely to be because plants are under constant evolutionary pressure to produce complex chemistry for communication and defense.”
Environmental engineers at Washington University in St. Louis develop critical methods to remove toxic selenium from water.