INVESTIGADORES
RODRIGUEZ Fernanda Mariana
artículos
Título:
Structure of the TatC core of the twin-arginine protein transport system
Autor/es:
SARAH E. ROLLAUER; MICHAEL J. TARRY; JAMES E. GRAHAM; MARI JÄÄSKELÄINEN; FRANZISKA JÄGER; STEVEN JOHNSON; MARTIN KREHENBRINK; SAI-MAN LIU; MICHAEL J. LUKEY; JULIEN MARCOUX; MELANIE A. MCDOWELL; FERNANDA RODRIGUEZ; PIETRO ROVERSI; PHILLIP J. STANSFELD; CAROL V. ROBINSON; MARK S. P. SANSOM; TRACY PALMER; MARTIN HÖGBOM; BEN C. BERKS; SUSAN M. LEA
Revista:
NATURE
Editorial:
NATURE PUBLISHING GROUP
Referencias:
Lugar: Londres; Año: 2012 vol. 492 p. 210 - 214
ISSN:
0028-0836
Resumen:
The twin-arginine translocation (Tat) pathway is one of two general protein transport systems found in the prokaryotic cytoplasmic membrane and is conserved in the thylakoid membrane of plant chloroplasts. The defining, and highly unusual, property of the Tat pathway is that it transports folded proteins, atask that must be achieved without allowing appreciable ion leakage across the membrane. The integral membrane TatC protein is the central component of the Tat pathway. TatC captures substrate proteins by binding their signal peptides. TatC then recruits TatA family proteins to form the active translocation complex. Here we report the crystal structure of TatC from the hyperthermophilic bacterium Aquifex aeolicus. This structure provides a molecular description of the core of the Tat translocation system and a framework for understanding the unique Tat transport mechanism.