Publication

Lipids activate SecA for high affinity binding to the SecYEG complex

Koch, S., de Wit, J. G., Vos, I., Birkner, J. P., Gordiichuk, P., Herrmann, A., van Oijen, A. M. & Driessen, A. J. M., 21-Oct-2016, In : The Journal of Biological Chemistry. 291, 43, p. 22534-22543 9 p.

Research output: Contribution to journalArticleAcademicpeer-review

APA

Koch, S., de Wit, J. G., Vos, I., Birkner, J. P., Gordiichuk, P., Herrmann, A., ... Driessen, A. J. M. (2016). Lipids activate SecA for high affinity binding to the SecYEG complex. The Journal of Biological Chemistry, 291(43), 22534-22543. https://doi.org/10.1074/jbc.M116.743831

Author

Koch, Sabrina ; de Wit, Janny G. ; Vos, Iuliia ; Birkner, Jan Peter ; Gordiichuk, Pavlo ; Herrmann, Andreas ; van Oijen, Antoine M ; Driessen, Arnold J.M. / Lipids activate SecA for high affinity binding to the SecYEG complex. In: The Journal of Biological Chemistry. 2016 ; Vol. 291, No. 43. pp. 22534-22543.

Harvard

Koch, S, de Wit, JG, Vos, I, Birkner, JP, Gordiichuk, P, Herrmann, A, van Oijen, AM & Driessen, AJM 2016, 'Lipids activate SecA for high affinity binding to the SecYEG complex', The Journal of Biological Chemistry, vol. 291, no. 43, pp. 22534-22543. https://doi.org/10.1074/jbc.M116.743831

Standard

Lipids activate SecA for high affinity binding to the SecYEG complex. / Koch, Sabrina; de Wit, Janny G.; Vos, Iuliia; Birkner, Jan Peter; Gordiichuk, Pavlo; Herrmann, Andreas; van Oijen, Antoine M; Driessen, Arnold J.M.

In: The Journal of Biological Chemistry, Vol. 291, No. 43, 21.10.2016, p. 22534-22543.

Research output: Contribution to journalArticleAcademicpeer-review

Vancouver

Koch S, de Wit JG, Vos I, Birkner JP, Gordiichuk P, Herrmann A et al. Lipids activate SecA for high affinity binding to the SecYEG complex. The Journal of Biological Chemistry. 2016 Oct 21;291(43):22534-22543. https://doi.org/10.1074/jbc.M116.743831


BibTeX

@article{e4192cea89044c838e63dc5ca646bc18,
title = "Lipids activate SecA for high affinity binding to the SecYEG complex",
abstract = "Protein translocation across the bacterial cytoplasmic membrane is an essential process catalyzed predominantly by the Sec translocase. This system consists of the membrane-embedded protein-conducting channel SecYEG, the motor ATPase SecA, and the heterotrimeric SecDFyajC membrane protein complex. Previous studies suggest that anionic lipids are essential for SecA activity and that the N-terminus of SecA is capable of penetrating the lipid bilayer. The role of lipid binding, however, has remained elusive. By employing differently sized nanodiscs reconstituted with single SecYEG complexes and comprising varying amounts of lipids, we establish that SecA gains access to the SecYEG complex via a lipid-bound intermediate state, whilst acidic phospholipids allosterically activate SecA for ATP-dependent protein translocation.",
keywords = "DEPENDENT MANNER, ATPASE, COLI PLASMA-MEMBRANE, ESCHERICHIA-COLI, PROTEIN-TRANSLOCATION, IN-VIVO, NANOLIPOPROTEIN PARTICLES, PREPROTEIN TRANSLOCASE, PHOSPHOLIPID-BILAYER, ACIDIC PHOSPHOLIPIDS",
author = "Sabrina Koch and {de Wit}, {Janny G.} and Iuliia Vos and Birkner, {Jan Peter} and Pavlo Gordiichuk and Andreas Herrmann and {van Oijen}, {Antoine M} and Driessen, {Arnold J.M.}",
note = "Copyright {\circledC} 2016, The American Society for Biochemistry and Molecular Biology.",
year = "2016",
month = "10",
day = "21",
doi = "10.1074/jbc.M116.743831",
language = "English",
volume = "291",
pages = "22534--22543",
journal = "The Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC",
number = "43",

}

RIS

TY - JOUR

T1 - Lipids activate SecA for high affinity binding to the SecYEG complex

AU - Koch, Sabrina

AU - de Wit, Janny G.

AU - Vos, Iuliia

AU - Birkner, Jan Peter

AU - Gordiichuk, Pavlo

AU - Herrmann, Andreas

AU - van Oijen, Antoine M

AU - Driessen, Arnold J.M.

N1 - Copyright © 2016, The American Society for Biochemistry and Molecular Biology.

PY - 2016/10/21

Y1 - 2016/10/21

N2 - Protein translocation across the bacterial cytoplasmic membrane is an essential process catalyzed predominantly by the Sec translocase. This system consists of the membrane-embedded protein-conducting channel SecYEG, the motor ATPase SecA, and the heterotrimeric SecDFyajC membrane protein complex. Previous studies suggest that anionic lipids are essential for SecA activity and that the N-terminus of SecA is capable of penetrating the lipid bilayer. The role of lipid binding, however, has remained elusive. By employing differently sized nanodiscs reconstituted with single SecYEG complexes and comprising varying amounts of lipids, we establish that SecA gains access to the SecYEG complex via a lipid-bound intermediate state, whilst acidic phospholipids allosterically activate SecA for ATP-dependent protein translocation.

AB - Protein translocation across the bacterial cytoplasmic membrane is an essential process catalyzed predominantly by the Sec translocase. This system consists of the membrane-embedded protein-conducting channel SecYEG, the motor ATPase SecA, and the heterotrimeric SecDFyajC membrane protein complex. Previous studies suggest that anionic lipids are essential for SecA activity and that the N-terminus of SecA is capable of penetrating the lipid bilayer. The role of lipid binding, however, has remained elusive. By employing differently sized nanodiscs reconstituted with single SecYEG complexes and comprising varying amounts of lipids, we establish that SecA gains access to the SecYEG complex via a lipid-bound intermediate state, whilst acidic phospholipids allosterically activate SecA for ATP-dependent protein translocation.

KW - DEPENDENT MANNER

KW - ATPASE

KW - COLI PLASMA-MEMBRANE

KW - ESCHERICHIA-COLI

KW - PROTEIN-TRANSLOCATION

KW - IN-VIVO

KW - NANOLIPOPROTEIN PARTICLES

KW - PREPROTEIN TRANSLOCASE

KW - PHOSPHOLIPID-BILAYER

KW - ACIDIC PHOSPHOLIPIDS

U2 - 10.1074/jbc.M116.743831

DO - 10.1074/jbc.M116.743831

M3 - Article

VL - 291

SP - 22534

EP - 22543

JO - The Journal of Biological Chemistry

JF - The Journal of Biological Chemistry

SN - 0021-9258

IS - 43

ER -

ID: 35343167