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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 Helmann1
1Department of Microbiology, Cornell University, 370 Wing Hall, 123 Wing Drive, Ithaca, New York 14853-8101, USA.
TerC family proteins, like MeeF and MeeY, are crucial for metalating exported enzymes, particularly manganese-dependent ones, ensuring proper protein function. Their absence impairs protein export and manganese levels in secreted proteins.
Area of Science:
- Microbiology
- Biochemistry
- Molecular Biology
Background:
- Cytosolic metalloenzymes obtain metals intracellularly, but the mechanism for metalating exported enzymes is less understood.
- Proper metalation is essential for the function of many secreted and membrane-associated enzymes.
Approach:
- Investigated the role of TerC family proteins, specifically MeeF(YceF) and MeeY(YkoY) in Bacillus subtilis, in enzyme metalation during secretion.
- Utilized genetic knockouts and copurification assays to analyze protein interactions and cellular functions.
- Assessed the impact of MeeF/MeeY absence on protein export capacity, manganese levels in the secreted proteome, and the function of manganese-dependent enzymes like LtaS.
Key Points:
- Bacillus subtilis strains lacking MeeF and MeeY exhibit reduced protein export and significantly lower manganese levels in secreted proteins.
- MeeF and MeeY associate with components of the general secretory pathway.
- The absence of MeeF and MeeY renders the FtsH membrane protease essential for cell viability and impairs the function of manganese-dependent lipoteichoic acid synthase (LtaS).
Conclusions:
- MeeF and MeeY, members of the conserved TerC family, facilitate the co-translocational metalation of enzymes during their export via the general secretion pathway.
- These proteins are vital for the proper manganese (Mn) incorporation into membrane-bound and extracellular enzymes, ensuring their functional activity.
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