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Essential protein SepF of mycobacteria interacts with FtsZ and MurG to regulate cell growth and division

Shamba Gupta1, Srijon Kaushik Banerjee1, Ayan Chatterjee1

  • 1Department of Chemistry, Bose Institute, 93/1 Acharya Prafulla Chandra Road, Kolkata 700009, India.

Microbiology (Reading, England)
|May 15, 2015
PubMed

Insights

Mycobacterium tuberculosis protein SepF is essential for bacterial cell division. SepF interacts with FtsZ and MurG, linking cell division and cell wall synthesis.

Area of Science:

  • Microbiology
  • Molecular Biology
  • Cell Biology

Background:

  • Bacterial cell division and cell wall biosynthesis are coordinated processes.
  • Protein complexes regulate these processes temporally and spatially.
  • Key players in mycobacterial cell division complexes are not fully understood.

Purpose of the Study:

  • To identify and characterize novel components of the mycobacterial cell division machinery.
  • To investigate the role of Rv2147c (SepF) in Mycobacterium tuberculosis cell division.

Main Methods:

  • In vitro and in vivo interaction assays.
  • Mutagenesis to identify key amino acid residues.
  • Functional studies using Mycobacterium smegmatis as a surrogate system.
  • Gene knockdown experiments.

Main Results:

  • Rv2147c (SepF) interacts with FtsZ, the primary cytokinesis driver.
  • Specific amino acid residues (189A, 190K, 215F) are crucial for FtsZ-SepF interaction.
  • SepF self-interaction was observed both in vitro and in vivo.
  • sepF is essential in Mycobacterium smegmatis.
  • SepF knockdown caused cell elongation, growth defects, and FtsZ mislocalization.
  • SepF interacts with MurG, a peptidoglycan synthesis enzyme.

Conclusions:

  • SepF is a newly identified essential component of the mycobacterial cell division complex.
  • SepF plays a critical role in coordinating cell division and cell wall synthesis.
  • SepF likely acts as a scaffold, linking FtsZ and peptidoglycan synthesis machinery.

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