Non-coding nucleotides and amino acids near the active site regulate peptide deformylase expression and inhibitor susceptibility in Chlamydia trachomatis Academic Article uri icon


MeSH Major

  • Amidohydrolases
  • Chlamydia trachomatis
  • Gene Expression Regulation, Bacterial


  • Chlamydia trachomatis, an obligate intracellular bacterium, is a highly prevalent human pathogen. Hydroxamic-acid-based matrix metalloprotease inhibitors can effectively inhibit the pathogen both in vitro and in vivo, and have exhibited therapeutic potential. Here, we provide genome sequencing data indicating that peptide deformylase (PDF) is the sole target of the inhibitors in this organism. We further report molecular mechanisms that control chlamydial PDF (cPDF) expression and inhibition efficiency. In particular, we identify the σ⁶⁶-dependent promoter that controls cPDF gene expression and demonstrate that point mutations in this promoter lead to resistance by increasing cPDF transcription. Furthermore, we show that substitution of two amino acids near the active site of the enzyme alters enzyme kinetics and protein stability.

publication date

  • September 2011



  • Academic Article



  • eng

PubMed Central ID

  • PMC3352175

Digital Object Identifier (DOI)

  • 10.1099/mic.0.049668-0

PubMed ID

  • 21719536

Additional Document Info

start page

  • 2569

end page

  • 81


  • 157


  • 9