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Polypeptide functionalized gold nanoprobes for SERS-fluorescence detection and imaging of caspase-9 during apoptosis.
Anal Chim Acta
January 2025
State Key Laboratory of Food Science and Resources, Jiangnan University, Wuxi, 214122, China; School of Food Science and Technology, Jiangnan University, Wuxi, 214122, China; International Joint Laboratory on Food Safety, Jiangnan University, Wuxi, 214122, China; Collaborative Innovation Center of Food Safety and Quality Control in Jiangsu Province, Jiangnan University, Wuxi, 214122, China.
Article Synopsis
- Deoxynivalenol (DON) is a common fungal toxin found in processed grain foods, associated with cytotoxic effects that lead to apoptosis and disrupt protein synthesis, making monitoring of caspase activity crucial.
- A novel gold nanoprobe designed for real-time detection of caspase-9 during DON-induced apoptosis was created, utilizing polypeptides and nanostars to enhance sensitivity and signal detection.
- This method allows for dual signal quantification and visualization of caspase-9 in living cells, advancing research on food safety and cellular mechanisms with applications across various human cell lines.
Deciphering the SAM- and metal-dependent mechanism of O-methyltransferases in cystargolide and belactosin biosynthesis: A structure-activity relationship study.
J Biol Chem
September 2024
Department of Bioscience, Center for Protein Assemblies (CPA), TUM School of Natural Sciences, Technical University of Munich, Garching, Germany. Electronic address:
Article Synopsis
- Cystargolides and belactosins are natural compounds that inhibit proteases, making them potential treatments for cancers and neurodegenerative diseases.
- Recent genetic analyses suggest that these inhibitors share similarities in their biosynthetic pathways.
- Researchers identified a specific motif (His-His-Asp) in enzymes BelI and CysG that is essential for function, revealing a unique metal-dependent mechanism in their synthesis.
Targeting New Functions and Applications of Bacterial Two-Component Systems.
Chembiochem
October 2024
Wuhan National Laboratory for Optoelectronics, Huazhong University of Science and Technology, Wuhan, 430074, China.
Two-component signal transduction systems (TCSs) are regulatory systems widely distributed in eubacteria, archaea, and a few eukaryotic organisms, but not in mammalian cells. A typical TCS consists of a histidine kinase and a response regulator protein. Functional and mechanistic studies on different TCSs have greatly advanced the understanding of cellular phosphotransfer signal transduction mechanisms.
View Article and Find Full Text PDFLegionella effectors SidC/SdcA ubiquitinate multiple small GTPases and SNARE proteins to promote phagosomal maturation.
Cell Mol Life Sci
June 2024
State Key Laboratory for Diagnosis and Treatment of Severe Zoonotic Infectious Diseases, Key Laboratory for Zoonosis Research of the Ministry of Education, College of Veterinary Medicine, Jilin University, Center for Pathogen Biology and Infectious Diseases, The First Hospital of Jilin University, Changchun, China.
Protein ubiquitination is one of the most important posttranslational modifications (PTMs) in eukaryotes and is involved in the regulation of almost all cellular signaling pathways. The intracellular bacterial pathogen Legionella pneumophila translocates at least 26 effectors to hijack host ubiquitination signaling via distinct mechanisms. Among these effectors, SidC/SdcA are novel E3 ubiquitin ligases with the adoption of a Cys-His-Asp catalytic triad.
View Article and Find Full Text PDFCopper interaction with cystatin C: effects on protein structure and oligomerization.
FEBS J
May 2024
Department of Biomedical Chemistry, Faculty of Chemistry, University of Gdańsk, Poland.
Article Synopsis
- Human cystatin C (hCC) has potential roles in neurodegenerative disorders beyond being a cysteine protease inhibitor, prompting investigation into its interaction with copper(II) ions (Cu(II)).
- Various techniques demonstrated that while Cu(II) ions do not alter the structure of hCC, they significantly affect its stability and oligomerization, particularly through specific histidine residues that bind copper.
- The study identifies critical Cu(II)-binding sites in hCC, linking copper's impact on protein stability to broader implications for understanding neurodegenerative diseases and developing potential therapies.
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