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Published on: August 10, 2021
TerC proteins function during protein secretion to metalate exoenzymes
Bixi He1, Ankita J Sachla1, John D Helmann2
1Department of Microbiology, Cornell University, 370 Wing Hall, 123 Wing Drive, Ithaca, NY, 14853-8101, USA.
TerC family proteins, like MeeF and MeeY, are crucial for metalating exported enzymes, particularly manganese-dependent ones, ensuring proper protein function during secretion.
Area of Science:
- Microbiology
- Biochemistry
- Molecular Biology
Background:
- Cytosolic metalloenzymes obtain metals intracellularly.
- Mechanisms for metalating extracellular enzymes via secretion pathways are not well understood.
Purpose of the Study:
- To investigate the role of TerC family proteins in the metalation of exported enzymes.
- To elucidate the function of MeeF and MeeY in the general secretion pathway and manganese homeostasis.
Main Methods:
- Investigated Bacillus subtilis strains lacking MeeF(YceF) and MeeY(YkoY).
- Analyzed protein export capacity and manganese levels in the secreted proteome.
- Examined copurification of MeeF/MeeY with general secretory pathway components.
- Assessed the impact on manganese-dependent lipoteichoic acid synthase (LtaS) function.
Main Results:
- Absence of MeeF and MeeY reduced protein export and secreted manganese levels.
- MeeF and MeeY interact with the general secretory pathway.
- FtsH membrane protease became essential for viability in MeeF/MeeY deficient strains.
- MeeF and MeeY are required for efficient manganese delivery to LtaS.
Conclusions:
- TerC family proteins, exemplified by MeeF and MeeY, facilitate co-translocational metalation of enzymes during general secretion.
- This process is vital for manganese-dependent membrane and extracellular enzymes, including LtaS.
- MeeF and MeeY play a critical role in manganese homeostasis for secreted proteins.
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