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Elongation factor Tu is a multifunctional and processed moonlighting protein.

Michael Widjaja1, Kate Louise Harvey1, Lisa Hagemann2

  • 1The ithree institute, University of Technology Sydney, PO Box 123, Broadway, NSW, 2007, Australia.

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Bacterial Elongation factor Tu (Ef-Tu) moonlights on pathogen surfaces, binding host molecules and aiding in virulence. Protein processing and positively charged residues in short linear motifs (SLiMs) drive this multifunctional behavior.

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Area of Science:

  • Microbiology
  • Molecular Biology
  • Biochemistry

Background:

  • Moonlighting proteins, performing multiple functions, are common in low G+C Firmicutes.
  • Elongation factor Tu (Ef-Tu) is a crucial protein in bacterial translation.

Purpose of the Study:

  • To investigate the moonlighting functions of Elongation factor Tu (Ef-Tu) on the surface of bacterial pathogens.
  • To characterize the processing and host-binding capabilities of surface-exposed Ef-Tu.

Main Methods:

  • N-terminomics pipeline to identify protein processing sites.
  • Recombinant protein expression and binding assays.
  • Bioinformatics and structural modeling.

Main Results:

  • Ef-Tu identified on the surface of Staphylococcus aureus, Mycoplasma pneumoniae, and Mycoplasma hyopneumoniae.
  • Surface-exposed Ef-Tu undergoes processing events.
  • Recombinant Ef-Tu binds host molecules, including plasminogen, and exhibits enzymatic activity.
  • Positively charged amino acids in short linear motifs (SLiMs) and protein processing contribute to moonlighting.

Conclusions:

  • Bacterial Ef-Tu exhibits moonlighting functions on the cell surface, contributing to pathogen virulence.
  • Protein processing and accumulation of positive charges in SLiMs are key mechanisms for Ef-Tu's multifunctional behavior.
  • Genome composition may influence the evolution of these moonlighting traits.