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- Title
FtsA G50E mutant suppresses the essential requirement for FtsK during bacterial cell division in Escherichia coli.
- Authors
Berezuk, Alison M.; Roach, Elyse J.; Seidel, Laura; Lo, Reggie Y.; Khursigara, Cezar M.
- Abstract
In Escherichia coli, the N-terminal domain of the essential protein FtsK (FtsKN) 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.
- Subjects
ESCHERICHIA coli; BACTERIAL cells; PROTEIN-protein interactions; CELL morphology; SITE-specific mutagenesis
- Publication
Canadian Journal of Microbiology, 2020, Vol 66, Issue 4, p313
- ISSN
0008-4166
- Publication type
Article
- DOI
10.1139/cjm-2019-0493