1. FtsA G50E mutant suppresses the essential requirement for FtsK during bacterial cell division in Escherichia coli .
- Author
-
Berezuk AM, Roach EJ, Seidel L, Lo RY, and Khursigara CM
- Subjects
- Escherichia coli cytology, Escherichia coli genetics, Escherichia coli Proteins genetics, Gene Expression Regulation, Bacterial, Membrane Proteins genetics, Mutagenesis, Mutation, Missense, Protein Binding, Cell Division, Escherichia coli metabolism, Escherichia coli Proteins metabolism, Membrane Proteins metabolism
- Abstract
In Escherichia coli , the N-terminal domain of the essential protein FtsK (FtsK
N ) is proposed to modulate septum formation through the formation of dynamic and essential protein interactions with both the Z-ring and late-stage division machinery. Using genomic mutagenesis, complementation analysis, and in vitro pull-down assays, we aimed to identify protein interaction partners of FtsK essential to its function during division. Here, we identified the cytoplasmic Z-ring membrane anchoring protein FtsA as a direct protein-protein interaction partner of FtsK. Random genomic mutagenesis of an ftsK temperature-sensitive strain of E . coli revealed an FtsA point mutation (G50E) that is able to fully restore normal cell growth and morphology, and further targeted site-directed mutagenesis of FtsA revealed several other point mutations capable of fully suppressing the essential requirement for functional FtsK. Together, this provides insight into a potential novel co-complex formed between these components during division and suggests FtsA may directly impact FtsK function.- Published
- 2020
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