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A small molecule allosterically activates SecA dependent secretion.

Haitham Sedky1,2, Mohamed Belal Hamed1,3, Srinath Krishnamurthy1

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A novel small molecule, HSI#6, activates the bacterial Sec translocase pathway independently of protein clients. This discovery provides the first Sec pathway activator and potential new antibacterial strategies.

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Area of Science:

  • Molecular Biology
  • Microbiology
  • Biochemistry

Background:

  • The Sec pathway is crucial for protein secretion in all organisms.
  • In bacteria, the SecA ATPase and SecYEG channel form the translocase for protein export.
  • Translocase activation relies on signal peptide and mature domain binding, coupling client selectivity with secretion.

Purpose of the Study:

  • To investigate the effect of the small molecule HSI#6 on the bacterial Sec translocase.
  • To determine if HSI#6 can activate the translocase independently of its protein clients.
  • To explore the potential of HSI#6 as a tool for understanding protein secretion and as an antibacterial lead.

Main Methods:

  • Biochemical assays to study SecA ATPase activity and translocase function.
  • In vitro and in vivo experiments to assess protein secretion efficiency.
  • Analysis of the allosteric effects of HSI#6 on translocase dynamics and client selectivity.

Main Results:

  • HSI#6 binds to SecA, modulating its dynamics and allosterically activating the translocase without clients.
  • This activation uncouples translocase activation from preprotein binding, leading to loss of client selectivity.
  • The translocase, when activated by HSI#6, efficiently secretes unfolded, premature, and cytoplasmic proteins both in vitro and in vivo.

Conclusions:

  • HSI#6 is the first identified activator of the Sec pathway.
  • This molecule transforms the translocase into a promiscuous nanomachine, highlighting the mechanism of client selectivity.
  • HSI#6 offers novel opportunities for antibacterial discovery by targeting the Sec pathway.