INVESTIGADORES
RODRIGUEZ fernanda Mariana
artículos
Título:
Structural model for the protein-translocating element of the twin-arginine transport system
Autor/es:
FERNANDA RODRIGUEZ; SARAH L. ROUSE; CLAUDIA TAIT; JEFFREY HARMER; ANTONIO DE RISO; CHRISTIANE R. TIMMEL; MARK S. P. SANSOM; BEN C. BERKS; JASON R. SCHNELL
Revista:
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Editorial:
NATL ACAD SCIENCES
Referencias:
Lugar: Washington DC, USA; Año: 2013 vol. 110 p. 1092 - 1101
ISSN:
0027-8424
Resumen:
The twin arginine translocase (Tat) carries out the remarkable process of translocating fully folded proteins across the cytoplasmic membrane of prokaryotes and the thylakoid membrane of plant chloroplasts. It is required for bacterial pathogenesis and for photosynthesis in plants. TatA, the protein-translocating element of the Tat system, is a small transmembrane protein that assembles into ring-like oligomers of variable size. We have determined a structural model of the Escherichia coli TatA complex by NMR. TatA assembly is mediated entirely by the transmembrane helix. The amphipathic helix extends outwards from the ring of transmembrane helices permitting assembly of complexes with variable subunit numbers. Transmembrane residue Gln8 points inwards resulting in a short hydrophobic pore in the centre of the complex. Simulations of the TatA complex in lipid bilayers indicate that the short transmembrane domain distorts the membrane. This suggests that TatA facilitates protein transport by sentitizing the membrane to transient rupture.