Life Sciences Commons^™

The Effect Of Glucose On Transcription At Cpxr- And Ompr-Regulated Promoters, Andrew Charles Cosgrove

Master's Theses

While reversible acetylation of proteins has been well studied in eukaryotes and is now recognized in bacteria, global protein acetylation in bacteria is a recently appreciated phenomenon. Protein acetylation is known to affect almost every aspect of cellular physiology in eukaryotes and there is proteomic evidence that this may also hold true in bacteria. In eukaryotes, lysines are acetylated by acetyltransferases that use acetyl-CoA as the acetyl group source, and de-acetylated by deacetylases. In bacteria, this reversible process uses enzymes homologous to those used by eukaryotes.

Our lab has recently found that acetylation of RNA polymerase (RNAP) can activate transcription …

Characterization Of The Clostridium Difficile Biofilm, Michelle Laning

Master's Theses

Clostridium difficile is a Gram-positive, spore forming bacterium and an opportunistic gastrointestinal pathogen. Clostridium difficile infection (CDI) is a common nosocomial infection. Upon antibiotic treatment, patients can be colonized with C. difficile from ingestion of spores. After colonization, cells produce toxins creating symptoms from diarrhea to pseudomembranous colitis, and many patients develop recurrent infections. Interactions between host epithelium and the bacteria is a critical step in infection, yet the interaction is not well understood. It is not known how C. difficile evades host immune responses. These are important mechanisms to answer in advancing CDI treatment. A biofilm could contribute to …

Understanding The Regulation Of Metabolic Enzyme Acetylation In E. Coli, Arti Walker-Peddakotla

Master's Theses

Global protein acetylation is a newly discovered phenomenon in bacteria. Of the more than 250 acetylations reported in E. coli, many are of metabolic enzymes. Thus, acetylation could represent a novel posttranslational mechanism of metabolic control. Yet, almost nothing is known about the regulation of these acetylations or of their metabolic outcomes. Here, we report that the cAMP receptor protein (CRP) regulates protein acetylation in E. coli and provide evidence that protein acetylation modulates the flux of carbon through central metabolism. When we grew cells in mixed amino acids supplemented with glucose and cAMP, global protein acetylation increased in a …