FtsA G50E mutant suppresses the essential requirement for FtsK during bacterial cell division in Escherichia coli.

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.

journal_name

Can J Microbiol

authors

Berezuk AM,Roach EJ,Seidel L,Lo RY,Khursigara CM

doi

10.1139/cjm-2019-0493

subject

Has Abstract

pub_date

2020-04-01 00:00:00

pages

313-327

issue

4

eissn

0008-4166

issn

1480-3275

journal_volume

66

pub_type

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