A5035989499- Bacterial Genetics and Biotechnology
- Bacterial Infections and Vaccines
- Enzyme Structure and Function
- Reproductive tract infections research
- Streptococcal Infections and Treatments
- Polyamine Metabolism and Applications
- Peptidase Inhibition and Analysis
- Bacteriophages and microbial interactions
- Antimicrobial Resistance in Staphylococcus
- Sirtuins and Resveratrol in Medicine
- RNA and protein synthesis mechanisms
- Adenosine and Purinergic Signaling
- Antimicrobial Peptides and Activities
- Autophagy in Disease and Therapy
- Invertebrate Immune Response Mechanisms
- Machine Learning in Bioinformatics
- Microbial Metabolic Engineering and Bioproduction
- Bacterial Identification and Susceptibility Testing
- Protein Structure and Dynamics
- Neurobiology and Insect Physiology Research
- Biochemical and Molecular Research
- Photosynthetic Processes and Mechanisms
- Oral microbiology and periodontitis research
- Biosensors and Analytical Detection
- Biochemical and Structural Characterization
Northwestern University
2020-2022
Loyola University Chicago
2010-2018
University of Wisconsin–Madison
2016-2018
The emerging view of Nε-lysine acetylation in eukaryotes is a relatively abundant post-translational modification (PTM) that has major impact on the function, structure, stability and/or location thousands proteins involved diverse cellular processes. This PTM typically considered to arise by donation acetyl group from acetyl-coenzyme A (acCoA) ε-amino lysine residue reversibly catalyzed acetyltransferases and deacetylases. Here, we provide genetic, mass spectrometric, biochemical structural...
Summary In E scherichia coli , acetylation of proteins at lysines depends largely on a non‐enzymatic acetyl phosphate‐dependent mechanism. To assess the functional significance this post‐translational modification, we first grew wild‐type cells in buffered tryptone broth with glucose and monitored over time by immunochemistry. Most occurred stationary phase paralleled consumption acetate excretion, which began upon entry into phase. Transcription rprA regulator, exhibited similar behavior....
Abstract N ε ‐lysine acetylation is an abundant posttranslational modification of thousands proteins involved in diverse cellular processes. In the model bacterium Escherichia coli , ‐amino group a lysine residue can be acetylated either catalytically by acetyl‐coenzyme A (acCoA) and acetyltransferases, or nonenzymatically acetyl phosphate (acP). It well known that catalytic acCoA‐dependent reversed deacetylases. Here, we provide genetic, mass spectrometric, structural immunological evidence...
Nε-lysine acetylation was recently discovered on many bacterial proteins that function in diverse cellular processes. Thus, questions remain unanswered. For example, what mechanisms regulate lysine acetylation? Does affect physiology? To help answer these questions, we studied the Escherichia coli response regulator and transcription factor RcsB, which is reported to be acetylated vitro. characterize RcsB acetylation, monitored from rprA promoter, requires RcsB. The conventional view...
An estimated 1.5 billion microbial infections occur globally each year and result in ∼4.6 million deaths. A technology gap associated with commercially available diagnostic tests remote underdeveloped regions prevents timely pathogen identification for effective antibiotic chemotherapies infected patients. The is a trial-and-error approach that limited effectiveness, increases risk patients while contributing to antimicrobial drug resistance, reduces the lifetime of antibiotics. This paper...
The Neisseria gonorrhoeae Type IV pilus is a multifunctional, dynamic fiber involved in host cell attachment, DNA transformation, and twitching motility. We previously reported that the N . also required for resistance against hydrogen peroxide-, antimicrobial peptide LL-37-, non-oxidative, neutrophil-mediated killing. tested whether peroxide, LL-37, neutrophil hypersensitivity phenotypes non-piliated could be due to elevated iron levels. Iron chelation growth medium rescued nonpiliated pilE...
Most bacterial species express one or more extracellular organelles called pili/fimbriae that are required for many properties of each cell. The Neisseria gonorrhoeae type IV pilus is a major virulence and colonization factor the sexually transmitted infection gonorrhea. We have discovered new protein TfpC to maintain pili on cell surface. There similar proteins found in other members genus important human health.
Spermidine N-acetyltransferase (SpeG) acetylates and thus neutralizes toxic polyamines. Studies indicate that SpeG plays an important role in virulence pathogenicity of many bacteria, which have evolved SpeG-dependent strategies to control polyamine concentrations survive their hosts. In Escherichia coli, the two-component response regulator RcsB is reported be subject Nε-acetylation on several lysine residues, resulting reduced DNA binding affinity transcription small RNA rprA; however,...
Abstract Neisseria gonorrhoeae rely on Type IV pili (T4p) to promote colonization of their human host and cause the sexually transmitted infection, gonorrhea. This organelle cycles through a process extension retraction back into bacterial cell. Through genetic screen, we identified NGO0783 locus N. strain FA1090 as containing gene encoding protein required stabilize pilus in its extended, non-retracted conformation. We have named tfpC TfpC. Deletion produces nonpiliated colony morphology...
Abstract Spermidine N -acetyltransferase (SpeG) acetylates and thus neutralizes toxic polyamines. Studies indicate that SpeG plays an important role in virulence pathogenicity of many bacteria, which have evolved SpeG-dependent strategies to control polyamine concentrations survive their hosts. In Escherichia coli , the two-component response regulator RcsB is reported be subject Nε-acetylation on several lysine residues, resulting reduced DNA binding affinity transcription small RNA rprA ;...