A5006694012- Prion Diseases and Protein Misfolding
- Monoclonal and Polyclonal Antibodies Research
- Microbial Metabolism and Applications
- Microbial Community Ecology and Physiology
- Neurological diseases and metabolism
- Trace Elements in Health
- Enzyme-mediated dye degradation
- Alzheimer's disease research and treatments
- Bacterial Genetics and Biotechnology
- Antibiotic Resistance in Bacteria
- Protein Structure and Dynamics
- Bacteriophages and microbial interactions
- Enzyme Structure and Function
University of Michigan
2024-2025
University of California, Santa Cruz
2019-2023
Fred Hutch Cancer Center
2022
North Seattle College
2022
Bacteriophage exclusion ('BREX') phage restriction systems are found in a wide range of bacteria. Various BREX encode unique combinations proteins that usually include site-specific methyltransferase; none appear to contain nuclease. Here we describe the identification and characterization Type I system from Acinetobacter effect deleting each ORF on growth, methylation, restriction. We identified previously uncharacterized gene operon is dispensable for methylation but involved Biochemical...
Encapsulins are self-assembling protein compartments found in prokaryotes and specifically encapsulate dedicated cargo enzymes. The most abundant encapsulin class Dye-decolorizing Peroxidases (DyPs). It has been previously suggested that DyP encapsulins involved oxidative stress resistance bacterial pathogenicity due to DyPs' inherent ability reduce detoxify hydrogen peroxide while oxidizing a broad range of organic co-substrates. Here, we report the structural biochemical analysis widely...
The C-terminal domain of the cellular prion protein (PrPC) contains two N-linked glycosylation sites, occupancy which impacts disease pathology. In this study, we demonstrate that glycans at these sites are required to maintain an intramolecular interaction with N-terminal domain, mediated through a previously identified copper-histidine tether, suppresses neurotoxic activity PrPC. NMR and electron paramagnetic resonance spectroscopy refine structure protein's interdomain interaction. Using...
Abstract The C-terminal domain of cellular prion protein (PrP C ) contains two N-linked glycosylation sites, the occupancy which impacts disease pathology. In this study, we demonstrate that glycans at these sites are required to maintain an intramolecular interaction with N-terminal domain, mediated through a previously identified copper-histidine tether, suppresses neurotoxic activity PrP . NMR and EPR spectroscopy refine structure protein’s interdomain interaction. Using whole-cell...
Encapsulins are self-assembling protein compartments found in prokaryotes and specifically encapsulate dedicated cargo enzymes. The most abundant encapsulin class Dye-decolorizing Peroxidases (DyPs). It has been previously suggested that DyP encapsulins involved oxidative stress resistance bacterial pathogenicity due to DyPs' inherent ability reduce detoxify hydrogen peroxide while oxidizing a broad range of organic co-substrates. Here, we report the structural biochemical analysis widely...
Bacterially expressed proteins used in NMR studies lack glycans, and from other organisms are neither 15N labeled nor glycosylated homogeneously. Here, we add two artificial glycans to uniformly prion protein using a buffer system that evolves over pH range accommodate the conflicting requirements of substrate enzymes without need fine-tune conditions. CD spectroscopy indicates do not influence its fold.