A5085397950- RNA and protein synthesis mechanisms
- Bacterial Genetics and Biotechnology
- Bacteriophages and microbial interactions
- Enzyme Structure and Function
- Protein Structure and Dynamics
- Trace Elements in Health
- Chemical Synthesis and Characterization
- Peptidase Inhibition and Analysis
- Radioactive element chemistry and processing
- Advanced Electron Microscopy Techniques and Applications
- Advanced biosensing and bioanalysis techniques
- Biochemical and Molecular Research
- Chemical Analysis and Environmental Impact
Dana-Farber Cancer Institute
2024
Harvard University
2024
University of Canterbury
2020-2024
Abstract Bacteria respond to environmental changes by inducing transcription of some genes and repressing others. Sialic acids, which coat human cell surfaces, are a nutrient source for pathogenic commensal bacteria. The Escherichia coli GntR-type transcriptional repressor, NanR, regulates sialic acid metabolism, but the mechanism is unclear. Here, we demonstrate that three NanR dimers bind (GGTATA) 3 -repeat operator cooperatively with high affinity. Single-particle cryo-electron microscopy...
Zinc is an essential micronutrient that regulates a wide range of physiological processes, most often through zinc binding to protein cysteine residues. Despite being critical for modulation function, the sites in majority human proteome are subject remain undefined. Here, we develop ZnCPT, deep and quantitative mapping zinc-binding proteome. We define 6,173 cysteines, uncovering families across major domains biology constitutive or inducible binding. ZnCPT enables systematic discovery...
Bacteria evolve mechanisms to compete for limited resources and survive in new niches. Here we study the mechanism of isethionate import from sulfate-reducing bacterium Oleidesulfovibrio alaskensis. The catabolism by Desulfovibrio species has been implicated human disease, due hydrogen sulfide production, potential industrial applications. O. alaskensis employs a tripartite ATP-independent periplasmic (TRAP) transporter (OaIsePQM) isethionate, which relies on substrate-binding protein...