Premium
Biochemical Characterization of MarR and TetR Proteins from Clostridium difficile
Author(s) -
Takahashi Rei,
Panchal Bhumika,
Kim Da Eun,
Wilkinson Steven
Publication year - 2018
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.2018.32.1_supplement.652.30
Subject(s) - tetr , clostridium difficile , pseudomembranous colitis , microbiology and biotechnology , biology , antibiotics , antibiotic resistance , clostridium , clostridium difficile colitis , pathogen , bacteria , computational biology , genetics , gene , transcription factor , repressor
Clostridium difficile , the causative agent of pseudomembranous colitis, is a leading cause of hospital acquired infections in the United States with approximately 420,000 – 700,000 new infections each year. Of major concern is the increasing rate of patient mortality and the rise in C. difficile infections in traditionally low‐risk groups (e.g. otherwise healthy adults) marked by the emergence of hypervirulent strains characterized by increased resistance to a range of antibiotics. In this study, we report initial efforts to purify and characterize MarR ( m ultiple a ntibiotic r esistance r egulator) and TetR ( tet racycline resistance r egulator) proteins from C. difficile as part of a larger investigation into the possible roles of these proteins in the antibiotic resistance mechanisms of this pathogen. MarR and TetR proteins are known to regulate genes required for antibiotic resistance in a number bacterial species but their functions in C. difficile remain unknown. A common feature of members of these two protein families is the specific binding of small‐molecule ligand(s) with accompanying changes in protein conformation and altered DNA‐binding affinity. Here we report initial results from analytical size exclusion to characterize the oligomerization states of C. difficile MarR and TetR proteins and results from biochemical analyses to characterize DNA‐binding. We also present results obtained from protein homology modeling with a particular focus on the conservation of residues in potential ligand‐binding sites and predicted DNA binding domains. Support or Funding Information California Polytechnical State University Research, Scholarly and Creative Activities Grant This abstract is from the Experimental Biology 2018 Meeting. There is no full text article associated with this abstract published in The FASEB Journal .