Disruption of divisome assembly rescued by FtsN-FtsA interaction in Escherichia coli.
Proc Natl Acad Sci U S A
; 115(29): E6855-E6862, 2018 07 17.
Article
em En
| MEDLINE
| ID: mdl-29967164
ABSTRACT
Cell division requires the assembly of a protein complex called the divisome. The divisome assembles in a hierarchical manner, with FtsA functioning as a hub to connect the Z-ring with the rest of the divisome and FtsN arriving last to activate the machine to synthesize peptidoglycan. FtsEX arrives as the Z-ring forms and acts on FtsA to initiate recruitment of the other divisome components. In the absence of FtsEX, recruitment is blocked; however, a multitude of conditions allow FtsEX to be bypassed. Here, we find that all such FtsEX bypass conditions, as well as the bypass of FtsK, depend upon the interaction of FtsN with FtsA, which promotes the back-recruitment of the late components of the divisome. Furthermore, our results suggest that these bypass conditions enhance the weak interaction of FtsN with FtsA and its periplasmic partners so that the divisome proteins are brought to the Z-ring when the normal hierarchical pathway is disrupted.
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Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Divisão Celular
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Periplasma
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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:
2018
Tipo de documento:
Article