Publication

The lateral gate of SecYEG opens during protein translocation.

du Plessis, D. J. F., Berrelkamp, G., Nouwen, N. P. & Driessen, A. J. M., 5-Jun-2009, In : The Journal of Biological Chemistry. 284, 23, p. 15805-15814 10 p.

Research output: Contribution to journalArticleAcademicpeer-review

APA

du Plessis, D. J. F., Berrelkamp, G., Nouwen, N. P., & Driessen, A. J. M. (2009). The lateral gate of SecYEG opens during protein translocation. The Journal of Biological Chemistry, 284(23), 15805-15814. https://doi.org/10.1074/jbc.M901855200

Author

du Plessis, D.J.F. ; Berrelkamp, G. ; Nouwen, N.P ; Driessen, A.J.M. / The lateral gate of SecYEG opens during protein translocation. In: The Journal of Biological Chemistry. 2009 ; Vol. 284, No. 23. pp. 15805-15814.

Harvard

du Plessis, DJF, Berrelkamp, G, Nouwen, NP & Driessen, AJM 2009, 'The lateral gate of SecYEG opens during protein translocation.', The Journal of Biological Chemistry, vol. 284, no. 23, pp. 15805-15814. https://doi.org/10.1074/jbc.M901855200

Standard

The lateral gate of SecYEG opens during protein translocation. / du Plessis, D.J.F.; Berrelkamp, G.; Nouwen, N.P; Driessen, A.J.M.

In: The Journal of Biological Chemistry, Vol. 284, No. 23, 05.06.2009, p. 15805-15814.

Research output: Contribution to journalArticleAcademicpeer-review

Vancouver

du Plessis DJF, Berrelkamp G, Nouwen NP, Driessen AJM. The lateral gate of SecYEG opens during protein translocation. The Journal of Biological Chemistry. 2009 Jun 5;284(23):15805-15814. https://doi.org/10.1074/jbc.M901855200


BibTeX

@article{dd9c21256e4c4bc185adba06df01c636,
title = "The lateral gate of SecYEG opens during protein translocation.",
abstract = "The SecYEG translocon of Escherichia coli mediates the translocation of preproteins across the cytoplasmic membrane. Here, we have examined the role of the proposed lateral gate of the translocon in translocation. A dual cysteine cross-linking approach allowed the introduction of cross-linker arms of various lengths between adjoining aminoacyl positions of transmembrane segments 2b and 7 of the lateral gate. Oxidation and short spacer linkers that fix the gate in the closed state abolished preprotein translocation, whereas long spacer linkers support translocation. The cross-linking data further suggests that SecYEG lateral gate opening and activation of the SecA ATPase are coupled processes. It is concluded that lateral gate opening is a critical step during SecA-dependent protein translocation.",
keywords = "BACTERIAL CYTOPLASMIC MEMBRANE, ESCHERICHIA-COLI, CONDUCTING CHANNEL, PREPROTEIN TRANSLOCATION, CROSS-LINKING, CATALYTIC CYCLE, SECA PROTEIN, ATPASE, COMPLEX, OMPT",
author = "{du Plessis}, D.J.F. and G. Berrelkamp and N.P Nouwen and A.J.M. Driessen",
year = "2009",
month = jun,
day = "5",
doi = "10.1074/jbc.M901855200",
language = "English",
volume = "284",
pages = "15805--15814",
journal = "The Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC",
number = "23",

}

RIS

TY - JOUR

T1 - The lateral gate of SecYEG opens during protein translocation.

AU - du Plessis, D.J.F.

AU - Berrelkamp, G.

AU - Nouwen, N.P

AU - Driessen, A.J.M.

PY - 2009/6/5

Y1 - 2009/6/5

N2 - The SecYEG translocon of Escherichia coli mediates the translocation of preproteins across the cytoplasmic membrane. Here, we have examined the role of the proposed lateral gate of the translocon in translocation. A dual cysteine cross-linking approach allowed the introduction of cross-linker arms of various lengths between adjoining aminoacyl positions of transmembrane segments 2b and 7 of the lateral gate. Oxidation and short spacer linkers that fix the gate in the closed state abolished preprotein translocation, whereas long spacer linkers support translocation. The cross-linking data further suggests that SecYEG lateral gate opening and activation of the SecA ATPase are coupled processes. It is concluded that lateral gate opening is a critical step during SecA-dependent protein translocation.

AB - The SecYEG translocon of Escherichia coli mediates the translocation of preproteins across the cytoplasmic membrane. Here, we have examined the role of the proposed lateral gate of the translocon in translocation. A dual cysteine cross-linking approach allowed the introduction of cross-linker arms of various lengths between adjoining aminoacyl positions of transmembrane segments 2b and 7 of the lateral gate. Oxidation and short spacer linkers that fix the gate in the closed state abolished preprotein translocation, whereas long spacer linkers support translocation. The cross-linking data further suggests that SecYEG lateral gate opening and activation of the SecA ATPase are coupled processes. It is concluded that lateral gate opening is a critical step during SecA-dependent protein translocation.

KW - BACTERIAL CYTOPLASMIC MEMBRANE

KW - ESCHERICHIA-COLI

KW - CONDUCTING CHANNEL

KW - PREPROTEIN TRANSLOCATION

KW - CROSS-LINKING

KW - CATALYTIC CYCLE

KW - SECA PROTEIN

KW - ATPASE

KW - COMPLEX

KW - OMPT

U2 - 10.1074/jbc.M901855200

DO - 10.1074/jbc.M901855200

M3 - Article

VL - 284

SP - 15805

EP - 15814

JO - The Journal of Biological Chemistry

JF - The Journal of Biological Chemistry

SN - 0021-9258

IS - 23

ER -

ID: 1927138