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- W2947978047 abstract "Summary Bacteria tightly regulate intracellular zinc levels to ensure sufficient zinc to support essential functions, while preventing toxicity. The bacterial response to zinc limitation includes the expression of putative zinc metallochaperones belonging to subfamily 1 of the COG0523 family of G3E GTPases. However, the client proteins and the metabolic processes served by these chaperones are unclear. Here, we demonstrate that the Bacillus subtilis YciC zinc metallochaperone (here renamed ZagA for Z TP a ctivated G TPase A ) supports de novo folate biosynthesis under conditions of zinc limitation, and interacts directly with the zinc‐dependent GTP cyclohydrolase IA, FolE (GCYH‐IA). Furthermore, we identify a role for the alarmone ZTP, a modified purine biosynthesis intermediate, in the response to zinc limitation. ZTP, a signal of 10‐formyl‐tetrahydrofolate (10f‐THF) deficiency in bacteria, transiently accumulates as FolE begins to fail, stimulates the interaction between ZagA and FolE, and thereby helps to sustain folate synthesis despite declining zinc availability." @default.
- W2947978047 created "2019-06-07" @default.
- W2947978047 creator A5016572389 @default.
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- W2947978047 date "2019-06-11" @default.
- W2947978047 modified "2023-10-16" @default.
- W2947978047 title "<i>Bacillus subtilis</i> FolE is sustained by the ZagA zinc metallochaperone and the alarmone ZTP under conditions of zinc deficiency" @default.
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- W2947978047 doi "https://doi.org/10.1111/mmi.14314" @default.
- W2947978047 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6736736" @default.
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- W2947978047 hasPublicationYear "2019" @default.
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