FtsA G50E mutant suppresses the essential requirement for FtsK during bacterial cell division in Escherichia coli
In: Canadian Journal of Microbiology, Jg. 66 (2020-04-01), S. 313-327
Online
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Zugriff:
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.
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FtsA G50E mutant suppresses the essential requirement for FtsK during bacterial cell division in Escherichia coli
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Autor/in / Beteiligte Person: | Khursigara, Cezar M. ; Reggie Y.C. Lo ; Seidel, Laura ; Roach, Elyse J. ; Berezuk, Alison |
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Zeitschrift: | Canadian Journal of Microbiology, Jg. 66 (2020-04-01), S. 313-327 |
Veröffentlichung: | Canadian Science Publishing, 2020 |
Medientyp: | unknown |
ISSN: | 1480-3275 (print) ; 0008-4166 (print) |
DOI: | 10.1139/cjm-2019-0493 |
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