A5072578759- Bacterial Genetics and Biotechnology
- Redox biology and oxidative stress
- Trace Elements in Health
- Enzyme Structure and Function
- bioluminescence and chemiluminescence research
- RNA and protein synthesis mechanisms
- CRISPR and Genetic Engineering
- Bacterial biofilms and quorum sensing
- Venomous Animal Envenomation and Studies
- Bacillus and Francisella bacterial research
- Viral Infectious Diseases and Gene Expression in Insects
- Metal-Catalyzed Oxygenation Mechanisms
- Endoplasmic Reticulum Stress and Disease
- Connexins and lens biology
- Environmental Toxicology and Ecotoxicology
- Iron Metabolism and Disorders
- Biochemical Acid Research Studies
- Electrochemical Analysis and Applications
- Wnt/β-catenin signaling in development and cancer
- Streptococcal Infections and Treatments
- Skin and Cellular Biology Research
- Glutathione Transferases and Polymorphisms
- Protein Structure and Dynamics
- Microbial Fuel Cells and Bioremediation
- Mitochondrial Function and Pathology
Bradley University
2012-2016
Cornell University
2010-2012
University of Illinois Urbana-Champaign
2011-2012
Harvard University
2006-2011
Harvard University Press
2008
Abstract Background Production of correctly disulfide bonded proteins to high yields remains a challenge. Recombinant protein expression in Escherichia coli is the popular choice, especially within research community. While there an ever growing demand for new strains, few strains are dedicated post-translational modifications, such as bond formation. Thus, must be engineered and parameters involved producing understood. Results We have E. strain named SHuffle, active its cytoplasm. This...
Summary Fur ( f erric u ptake r egulator) is the master regulator of iron homeostasis in many bacteria, but how it responds specifically to Fe II ) vivo not clear. Biochemical analyses B acillus subtilis BsFur reveal that addition ), both Z n( and Mn allosterically activate – DNA binding. Dimeric co‐purifies with site 1 structural Zn 2 can bind four additional or ions per dimer. Metal ion binding at previously described 3 occurs highest affinity, : Me form has only a modest increase affinity...
Escherichia coli expresses three types of ribonucleotide reductases (RNRs) that utilize the redox chemistry cysteine to catalyze reduction ribonucleotides. Upon reduction, cysteines form a disulfide bond and must be reduced. The authors present in vivo studies shed light on mechanism by which these enzymes are regenerated. class Ia enzyme, NrdAB, can reduced either thioredoxins 1 2 or glutaredoxin 1. Ib NrdEF, is dedicated glutaredoxin-like protein, NrdH. Despite its similarities...
In Escherichia coli, the glutathione/glutaredoxin and thioredoxin pathways are essential for reduction of cytoplasmic protein disulfide bonds, including those formed in enzyme ribonucleotide reductase during its action on substrates. Double mutants lacking (trxB) glutathione (gor) or biosynthesis (gshA) cannot grow. Growth Deltagor DeltatrxB strains is restored by a mutant (ahpC*) peroxiredoxin AhpC, converting it to that generates reduced glutathione. Here, we show ahpC* also restores...
Pasteurella multocida toxin (PMT) is an AB that causes pleiotropic effects in targeted host cells. The N-terminus of PMT (PMT-N) considered to harbor the membrane receptor binding and translocation domains responsible for mediating cellular entry delivery C-terminal catalytic domain into cytosol. Previous studies have implicated gangliosides as receptors binding. To gain further insight interactions involved cell membranes, we explored role various components binding, utilizing four...
In bacteria, cysteines of cytoplasmic proteins, including the essential enzyme ribonucleotide reductase (RNR), are maintained in reduced state by thioredoxin and glutathione/glutaredoxin pathways. An Escherichia coli mutant lacking both glutathione cannot grow because RNR is disulfide bonded nonfunctional. Here we report that suppressor mutations lpdA gene, which encodes oxidative lipoamide dehydrogenase required for tricarboxylic acid (TCA) cycle functioning, restore growth to this...
ABSTRACT Organisms growing aerobically generate reactive oxygen-containing molecules, such as hydrogen peroxide (H 2 O ). These oxygen molecules damage enzymes and DNA may even cause cell death. In response, Bacillus subtilis produces at least nine potential peroxide-scavenging enzymes, two of which appear to be the primary responsible for detoxifying peroxides during vegetative growth: a catalase (encoded by katA ) an alkylhydroperoxide reductase (Ahp, encoded ahpC AhpC uses redox-active...
The dermonecrotic toxins from Pasteurella multocida (PMT), Bordetella (DNT), Escherichia coli (CNF1-3) and Yersinia (CNFY) modulate their G-protein targets through deamidation and/or transglutamination of an active site Gln residue, which results in activation the G protein its cognate downstream signaling pathways. Whereas DNT CNFs act on small Rho GTPases, PMT acts α subunit heterotrimeric Gq, Gi G12/13 proteins. We previously demonstrated that potently blocks adipogenesis adipocyte...
Organisms growing aerobically generate reactive oxygen species such as hydrogen peroxide. These molecules damage enzymes and DNA, potentially causing cell death. In response, Bacillus subtilis produces at least nine potential peroxide-scavenging enzymes; two belong to the alkylhydroperoxide reductase (Ahp) class of peroxidases. Here, we explore role one these Ahp homologs, AhpA. While previous studies demonstrated that AhpA can scavenge peroxides thus defend cells against peroxides, they did...