Structural insights into a conserved mechanism of choline translocation and a distinct chaperonin-mediated protein folding cycle
- Autores: Jesús Vílchez García
- Directores de la Tesis: Jose Luis Nieva Escadón (dir. tes.), Iván Ubarrechena Belandia (codir. tes.)
- Lectura: En la Universidad del País Vasco - Euskal Herriko Unibertsitatea ( España ) en 2025
- Idioma: inglés
- Programa de doctorado: Programa de Doctorado en Biología Molecular y Biomedicina / Molecular Biology and Biomedicine por la Universidad del País Vasco/Euskal Herriko Unibertsitatea
- Menciones:
- Internacional
- Calificación: Sobresaliente Cum Laude
- Materias:
- Enlaces
- Tesis en acceso abierto en: ADDI
- Resumen
This thesis focuses on two distinct biological phenomena, following a structural biology approach based on cryo-electron microscopy (cryo-EM) for the determination of the high-resolution 3D structure of protein molecules: - The mechanism and evolutionary conservation of the Na+-dependent choline transport across biological membranes mediated by the transport protein CHT. We confirm the existence of a Na+- dependent choline transporter in bacteria homolog to human CHT. This transporter shares transport mechanism with the human counterpart, suggesting this mechanism appeared soon in evolution. - The distinct folding reaction cycle of the human mitochondrial mHsp60- mHsp10 chaperonin, with single- and double-ring pathways without negative inter-ring ATP-binding cooperativity, and the mechanism of mHsp10 lid ejection in absence of allosteric communication between mHsp60 rings.
