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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, facilitate manganese (Mn) metalation for secreted enzymes. This process is crucial for protein export and the function of Mn-dependent enzymes in Bacillus subtilis.
Area of Science:
- Microbiology
- Molecular Biology
- Biochemistry
Background:
- Cytosolic metalloenzymes obtain metals intracellularly, but mechanisms for metalating exported enzymes are unclear.
- The general secretion (Sec-dependent) pathway facilitates protein export across cellular membranes.
Approach:
- Investigated the role of MeeF(YceF) and MeeY(YkoY) proteins in Bacillus subtilis.
- Utilized copurification and genetic knockout studies.
- Assessed the impact on protein export, manganese levels in the secreted proteome, and the function of Mn-dependent enzymes like LtaS.
Key Points:
- Bacillus subtilis strains lacking MeeF and MeeY exhibit impaired protein export and significantly reduced manganese in secreted proteins.
- MeeF and MeeY associate with components of the general secretory pathway.
- Absence of MeeF and MeeY renders the FtsH membrane protease essential for cell viability.
- MeeF and MeeY are critical for the activity of the manganese-dependent enzyme LtaS.
Conclusions:
- MeeF and MeeY, members of the conserved TerC family, are essential for co-translocational metalation of enzymes during export via the Sec pathway.
- These proteins play a vital role in metalating manganese-dependent membrane and extracellular enzymes, ensuring their proper function.
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