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La microscopía de fuerza atómica de alta velocidad revela la catálisis rotatoria de la F1-ATPase sin rotor
Takayuki Uchihashi1, Ryota Iino, Toshio Ando
1Department of Physics, Kanazawa University, Kakuma-machi, Kanazawa 920-1192, Japan.
Science (New York, N.Y.)
|August 6, 2011
Resumen
El motor de la F(1)-ATPase es el motor de la F(1)-ATPase.
Área de la Ciencia:
- La bioquímica es la bioquímica.
- Biología Molecular Biología Molecular
- Biología Estructural Biología estructural.
Sus antecedentes:
- F(1)-ATPase es un motor rotativo impulsado por la hidrólisis del ATP.
- Su rotación unidireccional se basa en cambios conformacionales cooperativos en sus subunidades.
- La base estructural precisa para esta rotación unidireccional sigue sin estar clara.
Objetivo del estudio:
- Investigar las bases estructurales de la rotación unidireccional en la fase F-ATP.
- Para determinar si el anillo del estator por sí solo puede generar cambios de conformación direccional.
Principales métodos:
- Microscopía de fuerza atómica de alta velocidad (HS-AFM).
- Se estudió el anillo estatorizado aislado α(3) β(3) de F(1)-ATPasa sin el rotor (subunidad γ).
Principales resultados:
- El anillo del estator α(3) β(3) aislado exhibió "rotación" sin el rotor.
- Tres subunidades β se propagan cíclicamente en estados conformacionales en el sentido contrario a las agujas del reloj.
- Esta propagación conformacional imitaba el movimiento rotatorio del eje central F.
Conclusiones:
- La base estructural para la rotación unidireccional es inherente al anillo del estator.
- La interacción cooperativa entre las subunidades en el anillo del estator dicta la direccionalidad.
- Los hallazgos ofrecen información sobre otras ATPasas hexaméricas y la cooperación de subunidades.
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