Proteomic profiling of cellular stresses in Bacillus subtilis reveals cellular networks and assists in elucidating antibiotic mechanisms of action.
Proteomic profiling provides a global view of the protein composition of the cell. In contrast to the static nature of the genome sequence, which provides the blueprint for all protein-based cellular building blocks, the proteome is highly dynamic. The protein composition is constantly adjusting to facilitate survival, growth, and reproduction in an ever-changing environment. In a quest to understand the regulation of cellular networks in bacteria and the role of individual proteins in the adaptation process, the proteomic response to stress and starvation was analyzed in wild-type and mutant strains. The knowledge derived from these proteomic studies was applied to investigating the bacterial response to antibiotics. It was found that proteomics presents a powerful tool for hypothesis generation regarding antibiotic mechanism of action.
Bandow
Julia E
JE
Pfizer Global Research and Development, Pfizer Inc., Ann Arbor, Michigan, USA. julia.bandow@pfizer.com
Hecker
Michael
M
D000900:Anti-Bacterial Agents / Q000494:pharmacology* / Q000633:toxicity; D001412:Bacillus subtilis / Q000737:chemistry / Q000166:cytology / Q000187:drug effects* / Q000378:metabolism; D001426:Bacterial Proteins / Q000032:analysis / Q000096:biosynthesis*; D015195:Drug Design; D015180:Electrophoresis, Gel, Two-Dimensional; D013058:Mass Spectrometry; D008715:Methionine / Q000378:metabolism; D040901:Proteomics
D000900:Anti-Bacterial Agents; D001426:Bacterial Proteins; D008715:Methionine