INVESTIGADORES
RODRIGUEZ fernanda Mariana
congresos y reuniones científicas
Título:
Structural studies of oligomeric TatA by NMR
Autor/es:
FERNANDA RODRIGUEZ
Lugar:
Paris
Reunión:
Encuentro; CNRS-Oxford membrane protein meeting; 2012
Resumen:
<!--
/* Font Definitions */
@font-face
{font-family:Calibri;
panose-1:2 15 5 2 2 2 4 3 2 4;
mso-font-charset:0;
mso-generic-font-family:auto;
mso-font-pitch:variable;
mso-font-signature:3 0 0 0 1 0;}
@font-face
{font-family:Cambria;
panose-1:2 4 5 3 5 4 6 3 2 4;
mso-font-charset:0;
mso-generic-font-family:auto;
mso-font-pitch:variable;
mso-font-signature:3 0 0 0 1 0;}
/* Style Definitions */
p.MsoNormal, li.MsoNormal, div.MsoNormal
{mso-style-parent:"";
margin-top:0cm;
margin-right:0cm;
margin-bottom:10.0pt;
margin-left:0cm;
mso-pagination:widow-orphan;
font-size:12.0pt;
font-family:"Times New Roman";
mso-ascii-font-family:Cambria;
mso-ascii-theme-font:minor-latin;
mso-fareast-font-family:Cambria;
mso-fareast-theme-font:minor-latin;
mso-hansi-font-family:Cambria;
mso-hansi-theme-font:minor-latin;
mso-bidi-font-family:"Times New Roman";
mso-bidi-theme-font:minor-bidi;
mso-ansi-language:EN-US;}
@page Section1
{size:612.0pt 792.0pt;
margin:72.0pt 90.0pt 72.0pt 90.0pt;
mso-header-margin:36.0pt;
mso-footer-margin:36.0pt;
mso-paper-source:0;}
div.Section1
{page:Section1;}
-->
<!--
/* Font Definitions */
@font-face
{font-family:Arial;
panose-1:2 11 6 4 2 2 2 2 2 4;
mso-font-charset:0;
mso-generic-font-family:auto;
mso-font-pitch:variable;
mso-font-signature:3 0 0 0 1 0;}
@font-face
{font-family:Cambria;
panose-1:2 4 5 3 5 4 6 3 2 4;
mso-font-charset:0;
mso-generic-font-family:auto;
mso-font-pitch:variable;
mso-font-signature:3 0 0 0 1 0;}
/* Style Definitions */
p.MsoNormal, li.MsoNormal, div.MsoNormal
{mso-style-parent:"";
margin-top:0cm;
margin-right:0cm;
margin-bottom:10.0pt;
margin-left:0cm;
mso-pagination:widow-orphan;
font-size:12.0pt;
font-family:"Times New Roman";
mso-ascii-font-family:Cambria;
mso-ascii-theme-font:minor-latin;
mso-fareast-font-family:Cambria;
mso-fareast-theme-font:minor-latin;
mso-hansi-font-family:Cambria;
mso-hansi-theme-font:minor-latin;
mso-bidi-font-family:"Times New Roman";
mso-bidi-theme-font:minor-bidi;
mso-ansi-language:EN-US;}
@page Section1
{size:612.0pt 792.0pt;
margin:72.0pt 90.0pt 72.0pt 90.0pt;
mso-header-margin:36.0pt;
mso-footer-margin:36.0pt;
mso-paper-source:0;}
div.Section1
{page:Section1;}
-->
The twin arginine
translocase (Tat) moves folded proteins across the cytoplasmic membrane of
prokaryotes and the thylakoid membrane of plant chloroplasts. 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 used solution
state NMR to construct a high resolution model of the Escherichia coli TatA oligomer. TatA assembly is mediated entirely by
the transmembrane domain which form a pore enclosed by a ring of helices. Gln8
points in toward the symmetry axis, resulting in a short hydrophobic pore
lining. The TatA amphipathic helices extend outwards from the ring of
transmembrane helices. This mode of TatA assembly can accommodate a large
variation in the oligomeric state. Molecular dynamics simulations in lipid
bilayers indicate that the short transmembrane domain of TatA disrupts the membrane
in the oligomeric form. In contrast, monomeric TatA has an increased angle of
insertion into the membrane and a more deeply buried amphipathic helix, suggesting
that changes in TatA membrane insertion can regulate TatA assembly and activity.