FtsA G50E mutant suppresses the essential requirement for FtsK during bacterial cell division in Escherichia coli.
Can J Microbiol
; 66(4): 313-327, 2020 Apr.
Article
em En
| MEDLINE
| ID: mdl-31971820
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.
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Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Divisão Celular
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Proteínas de Escherichia coli
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Escherichia coli
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Proteínas de Membrana
Idioma:
En
Ano de publicação:
2020
Tipo de documento:
Article