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Crystal structure of FtsA from Staphylococcus aureus.

Junso Fujita1, Yoko Maeda1, Chioko Nagao2

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|April 22, 2014
PubMed
Summary

The bacterial cell division protein FtsA anchors FtsZ to the cell membrane. This study reveals the crystal structure of Staphylococcus aureus FtsA, showing its interaction with FtsZ enhances GTPase activity.

Keywords:
Bacterial divisomeFtsAFtsZStaphylococcus aureus

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Area of Science:

  • Microbiology
  • Structural Biology
  • Biochemistry

Background:

  • The bacterial cell-division protein FtsA is crucial for anchoring FtsZ to the cytoplasmic membrane, a key step in cell division.
  • The precise mechanism of FtsA and FtsZ interaction during membrane division is not fully understood.

Purpose of the Study:

  • To elucidate the structural basis of FtsA function in bacterial cell division.
  • To investigate the interaction between FtsA and FtsZ from Staphylococcus aureus and its effect on FtsZ activity.

Main Methods:

  • X-ray crystallography was used to determine the 2.2 Å resolution structure of FtsA from Staphylococcus aureus (SaFtsA).
  • In vitro biochemical assays were performed to confirm the association between SaFtsA and SaFtsZ.
  • GTPase activity assays were conducted to assess the impact of SaFtsA on SaFtsZ.

Main Results:

  • The crystal structure of SaFtsA revealed a twisted dimer conformation, differing from the straight filament observed in FtsA from Thermotoga maritima.
  • Half of the S12-S13 hairpin regions in SaFtsA were found to be disordered in the crystal structure.
  • In vitro experiments confirmed the association between SaFtsA and SaFtsZ.
  • Interaction with SaFtsA was found to enhance the GTPase activity of SaFtsZ.

Conclusions:

  • The structural and biochemical data provide new insights into the FtsA-FtsZ interaction at the molecular level.
  • The findings suggest a potential regulatory role for FtsA in modulating FtsZ GTPase activity, impacting bacterial cell division.
  • This study lays the groundwork for further investigations into the dynamic mechanisms of bacterial cytokinesis.