Cell division in Escherichia coli: role of FtsL domains in septal localization, function, and oligomerization.
J Bacteriol
; 182(1): 116-29, 2000 Jan.
Article
em En
| MEDLINE
| ID: mdl-10613870
ABSTRACT
In Escherichia coli, nine essential cell division proteins are known to localize to the division septum. FtsL is a 13-kDa bitopic membrane protein with a short cytoplasmic N-terminal domain, a membrane-spanning segment, and a periplasmic domain that has a repeated heptad motif characteristic of leucine zippers. Here, we identify the requirements for FtsL septal localization and function. We used green fluorescent protein fusions to FtsL proteins where domains of FtsL had been exchanged with analogous domains from either its Haemophilus influenzae homologue or the unrelated MalF protein to show that both the membrane-spanning segment and the periplasmic domain of FtsL are required for localization to the division site. Mutagenesis of the periplasmic heptad repeat motif severely impaired both localization and function as well as the ability of FtsL to drive the formation of sodium dodecyl sulfate-resistant multimers in vitro. These results are consistent with the predicted propensity of the FtsL periplasmic domain to adopt a coiled-coiled structure. This coiled-coil motif is conserved in all gram-negative and gram-positive FtsL homologues identified so far. Our data suggest that most of the FtsL molecule is a helical coiled coil involved in FtsL multimerization.
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Base de dados:
MEDLINE
Assunto principal:
Proteínas de Bactérias
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Proteínas de Transporte de Monossacarídeos
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Proteínas de Ciclo Celular
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Transportadores de Cassetes de Ligação de ATP
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Proteínas de Escherichia coli
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Proteínas Periplásmicas de Ligação
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Escherichia coli
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Proteínas de Membrana
Idioma:
En
Ano de publicação:
2000
Tipo de documento:
Article