Tol: Difference between revisions

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The Tol-Pal system is used by group A colicins in order to translocate across the outer membrane, targeting mainly the inner membrane component TolA as well as TolQ and TolR. The colicins set up a translocon, constituting of the outer membrane receptor, translocator proteins and one or more periplasmic translocator proteins. The colicins recruit the Tol proteins using a Tol binding antigen, or epitope, which is embedded in the IUTD (intrinsically unstructured translocation domain) found on the N-terminal (T-) domain of the colicin<ref>PMID: 21060316<ref/>.

The Tol-Pal system is used by group A colicins in order to translocate across the outer membrane, targeting mainly the inner membrane component TolA as well as TolQ and TolR. The colicins set up a translocon, constituting of the outer membrane receptor, translocator proteins and one or more periplasmic translocator proteins. The colicins recruit the Tol proteins using a Tol binding antigen, or epitope, which is embedded in the IUTD (intrinsically unstructured translocation domain) found on the N-terminal (T-) domain of the colicin<ref>PMID: 21060316</ref>.

A yeast two-hybrid screen was carried out in order to determine the interactions between colicins and the Tol-Pal system during the import of colicin.<ref name="Walburger">PMID: 11994151</ref> The screen showed that TolB dimerizes, and its amino terminal domain (D1) interacts with the periplasmic, C-terminal domain of TolA (TolAIII), whilst the central domain of TolA (TolAII) interacts with [[YbgF]]. It is the interaction between TolAIII and D1 that forms a "''trans''-envelope complex" which brings the inner and outer membranes closer together allowing for the uptake of colicin A. The N-terminal of the group A colicins then interact with TolA and also sometimes TolB during translocation into the inner membrane.

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 <structure load='2ivz' size='300' align='right' caption='Interaction of TolB and Colicin E9' (PDB entry [[2ivz]]  |  SCENE= Tol/Tolbcol/1 />
-The Tol-Pal system is used by group A colicins in order to translocate across the outer membrane, targeting mainly the inner membrane component TolA as well as TolQ and TolR.  The colicins set up a translocon, constituting of the outer membrane receptor, translocator proteins and one or more periplasmic translocator proteins.  The colicins recruit the Tol proteins using a Tol binding antigen, or epitope, which is embedded in the IUTD (intrinsically unstructured translocation domain) found on the N-terminal (T-) domain of the colicin<ref>PMID: 21060316<ref/>.
+The Tol-Pal system is used by group A colicins in order to translocate across the outer membrane, targeting mainly the inner membrane component TolA as well as TolQ and TolR.  The colicins set up a translocon, constituting of the outer membrane receptor, translocator proteins and one or more periplasmic translocator proteins.  The colicins recruit the Tol proteins using a Tol binding antigen, or epitope, which is embedded in the IUTD (intrinsically unstructured translocation domain) found on the N-terminal (T-) domain of the colicin<ref>PMID: 21060316</ref>.
 A yeast two-hybrid screen was carried out in order to determine the interactions between colicins and the Tol-Pal system during the import of colicin.<ref name="Walburger">PMID: 11994151</ref>  The screen showed that TolB dimerizes, and its amino terminal domain (D1) interacts with the periplasmic, C-terminal domain of TolA (TolAIII), whilst the central domain of TolA (TolAII) interacts with [[YbgF]].  It is the interaction between TolAIII and D1 that forms a "''trans''-envelope complex" which brings the inner and outer membranes closer together allowing for the uptake of colicin A.  The N-terminal of the group A colicins then interact with TolA and also sometimes TolB during translocation into the inner membrane.