Targeting and translocation of the two lipoproteins in Escherichia coli via the SRP/Sec/YidC pathway.

L. Froderberg, E.N.G. Houben, L Baars, S. Luirink, J.W. Gier de

Research output: Contribution to JournalArticleAcademicpeer-review

Abstract

In Escherichia coli, two main protein targeting pathways to the inner membrane exist: the SecB pathway for the essentially posttranslational targeting of secretory proteins and the SRP pathway for cotranslational targeting of inner membrane proteins (IMPs). At the inner membrane both pathways converge at the Sec translocase, which is capable of both linear transport into the periplasm and lateral transport into the lipid bilayer. The Sec-associated YidC appears to assist the lateral transport of IMPs from the Sec translocase into the lipid bilayer. It should be noted that targeting and translocation of only a handful of secretory proteins and IMPs have been studied. These model proteins do not include lipoproteins. Here, we have studied the targeting and translocation of two secretory lipoproteins, the murein lipoprotein and the bacteriocin release protein, using a combined in vivo and in vitro approach. The data indicate that both murein lipoprotein and bacteriocin release protein require the SRP pathway for efficient targeting to the Sec translocase. Furthermore, we show that YidC plays an important role in the targeting/translocation of both lipoproteins.
Original languageEnglish
Pages (from-to)31026-31032
Number of pages7
JournalJournal of Biological Chemistry
Volume279
DOIs
Publication statusPublished - 2004

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Escherichia coli
Lipoproteins
Bacteriocins
Peptidoglycan
Lipid Bilayers
Protein Transport
Membrane Proteins
Proteins
Lipid bilayers
Periplasm
Membranes
Membrane Transport Proteins

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@article{5509972f0ecf4506811da1986f8bc149,
title = "Targeting and translocation of the two lipoproteins in Escherichia coli via the SRP/Sec/YidC pathway.",
abstract = "In Escherichia coli, two main protein targeting pathways to the inner membrane exist: the SecB pathway for the essentially posttranslational targeting of secretory proteins and the SRP pathway for cotranslational targeting of inner membrane proteins (IMPs). At the inner membrane both pathways converge at the Sec translocase, which is capable of both linear transport into the periplasm and lateral transport into the lipid bilayer. The Sec-associated YidC appears to assist the lateral transport of IMPs from the Sec translocase into the lipid bilayer. It should be noted that targeting and translocation of only a handful of secretory proteins and IMPs have been studied. These model proteins do not include lipoproteins. Here, we have studied the targeting and translocation of two secretory lipoproteins, the murein lipoprotein and the bacteriocin release protein, using a combined in vivo and in vitro approach. The data indicate that both murein lipoprotein and bacteriocin release protein require the SRP pathway for efficient targeting to the Sec translocase. Furthermore, we show that YidC plays an important role in the targeting/translocation of both lipoproteins.",
author = "L. Froderberg and E.N.G. Houben and L Baars and S. Luirink and {Gier de}, J.W.",
year = "2004",
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language = "English",
volume = "279",
pages = "31026--31032",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
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Targeting and translocation of the two lipoproteins in Escherichia coli via the SRP/Sec/YidC pathway. / Froderberg, L.; Houben, E.N.G.; Baars, L; Luirink, S.; Gier de, J.W.

In: Journal of Biological Chemistry, Vol. 279, 2004, p. 31026-31032.

Research output: Contribution to JournalArticleAcademicpeer-review

TY - JOUR

T1 - Targeting and translocation of the two lipoproteins in Escherichia coli via the SRP/Sec/YidC pathway.

AU - Froderberg, L.

AU - Houben, E.N.G.

AU - Baars, L

AU - Luirink, S.

AU - Gier de, J.W.

PY - 2004

Y1 - 2004

N2 - In Escherichia coli, two main protein targeting pathways to the inner membrane exist: the SecB pathway for the essentially posttranslational targeting of secretory proteins and the SRP pathway for cotranslational targeting of inner membrane proteins (IMPs). At the inner membrane both pathways converge at the Sec translocase, which is capable of both linear transport into the periplasm and lateral transport into the lipid bilayer. The Sec-associated YidC appears to assist the lateral transport of IMPs from the Sec translocase into the lipid bilayer. It should be noted that targeting and translocation of only a handful of secretory proteins and IMPs have been studied. These model proteins do not include lipoproteins. Here, we have studied the targeting and translocation of two secretory lipoproteins, the murein lipoprotein and the bacteriocin release protein, using a combined in vivo and in vitro approach. The data indicate that both murein lipoprotein and bacteriocin release protein require the SRP pathway for efficient targeting to the Sec translocase. Furthermore, we show that YidC plays an important role in the targeting/translocation of both lipoproteins.

AB - In Escherichia coli, two main protein targeting pathways to the inner membrane exist: the SecB pathway for the essentially posttranslational targeting of secretory proteins and the SRP pathway for cotranslational targeting of inner membrane proteins (IMPs). At the inner membrane both pathways converge at the Sec translocase, which is capable of both linear transport into the periplasm and lateral transport into the lipid bilayer. The Sec-associated YidC appears to assist the lateral transport of IMPs from the Sec translocase into the lipid bilayer. It should be noted that targeting and translocation of only a handful of secretory proteins and IMPs have been studied. These model proteins do not include lipoproteins. Here, we have studied the targeting and translocation of two secretory lipoproteins, the murein lipoprotein and the bacteriocin release protein, using a combined in vivo and in vitro approach. The data indicate that both murein lipoprotein and bacteriocin release protein require the SRP pathway for efficient targeting to the Sec translocase. Furthermore, we show that YidC plays an important role in the targeting/translocation of both lipoproteins.

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DO - 10.1074/jbc.M403229200

M3 - Article

VL - 279

SP - 31026

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JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

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