The Min oscillator uses MinD-dependent conformational changes in MinE to spatially regulate cytokinesis.
Cell
; 146(3): 396-407, 2011 Aug 05.
Article
en En
| MEDLINE
| ID: mdl-21816275
ABSTRACT
In E. coli, MinD recruits MinE to the membrane, leading to a coupled oscillation required for spatial regulation of the cytokinetic Z ring. How these proteins interact, however, is not clear because the MinD-binding regions of MinE are sequestered within a six-stranded ß sheet and masked by N-terminal helices. minE mutations that restore interaction between some MinD and MinE mutants were isolated. These mutations alter the MinE structure leading to release of the MinD-binding regions and the N-terminal helices that bind the membrane. Crystallization of MinD-MinE complexes revealed a four-stranded ß sheet MinE dimer with the released ß strands (MinD-binding regions) converted to α helices bound to MinD dimers. These results identify the MinD-dependent conformational changes in MinE that convert it from a latent to an active form and lead to a model of how MinE persists at the MinD-membrane surface.
Texto completo:
1
Colección:
01-internacional
Banco de datos:
MEDLINE
Asunto principal:
Adenosina Trifosfatasas
/
Proteínas de Ciclo Celular
/
Proteínas de Escherichia coli
/
Escherichia coli
Idioma:
En
Revista:
Cell
Año:
2011
Tipo del documento:
Article
País de afiliación:
Estados Unidos