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TerC proteins function during protein secretion to metalate exoenzymes

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  • Bixi He

    (Cornell University)

  • Ankita J. Sachla

    (Cornell University)

  • John D. Helmann

    (Cornell University)

Abstract

Cytosolic metalloenzymes acquire metals from buffered intracellular pools. How exported metalloenzymes are appropriately metalated is less clear. We provide evidence that TerC family proteins function in metalation of enzymes during export through the general secretion (Sec-dependent) pathway. Bacillus subtilis strains lacking MeeF(YceF) and MeeY(YkoY) have a reduced capacity for protein export and a greatly reduced level of manganese (Mn) in the secreted proteome. MeeF and MeeY copurify with proteins of the general secretory pathway, and in their absence the FtsH membrane protease is essential for viability. MeeF and MeeY are also required for efficient function of the Mn2+-dependent lipoteichoic acid synthase (LtaS), a membrane-localized enzyme with an extracytoplasmic active site. Thus, MeeF and MeeY, representative of the widely conserved TerC family of membrane transporters, function in the co-translocational metalation of Mn2+-dependent membrane and extracellular enzymes.

Suggested Citation

  • Bixi He & Ankita J. Sachla & John D. Helmann, 2023. "TerC proteins function during protein secretion to metalate exoenzymes," Nature Communications, Nature, vol. 14(1), pages 1-13, December.
    • Handle: RePEc:nat:natcom:v:14:y:2023:i:1:d:10.1038_s41467-023-41896-1
    DOI: 10.1038/s41467-023-41896-1
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    1. Steve Tottey & Kevin J. Waldron & Susan J. Firbank & Brian Reale & Conrad Bessant & Katsuko Sato & Timothy R. Cheek & Joe Gray & Mark J. Banfield & Christopher Dennison & Nigel J. Robinson, 2008. "Protein-folding location can regulate manganese-binding versus copper- or zinc-binding," Nature, Nature, vol. 455(7216), pages 1138-1142, October.
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