Publication

Immobilization of the Plug Domain Inside the SecY Channel Allows Unrestricted Protein Translocation

Lycklama a Nijeholt, J. A., Bulacu, M., Marrink, S. J. & Driessen, A. J. M., 30-Jul-2010, In : The Journal of Biological Chemistry. 285, 31, p. 23747 - 23754 8 p.

Research output: Contribution to journalArticleAcademicpeer-review

APA

Lycklama a Nijeholt, J. A., Bulacu, M., Marrink, S. J., & Driessen, A. J. M. (2010). Immobilization of the Plug Domain Inside the SecY Channel Allows Unrestricted Protein Translocation. The Journal of Biological Chemistry, 285(31), 23747 - 23754. https://doi.org/10.1074/jbc.M110.124636

Author

Lycklama a Nijeholt, Jelger A. ; Bulacu, Monica ; Marrink, Siewert Jan ; Driessen, Arnold J.M. / Immobilization of the Plug Domain Inside the SecY Channel Allows Unrestricted Protein Translocation. In: The Journal of Biological Chemistry. 2010 ; Vol. 285, No. 31. pp. 23747 - 23754.

Harvard

Lycklama a Nijeholt, JA, Bulacu, M, Marrink, SJ & Driessen, AJM 2010, 'Immobilization of the Plug Domain Inside the SecY Channel Allows Unrestricted Protein Translocation', The Journal of Biological Chemistry, vol. 285, no. 31, pp. 23747 - 23754. https://doi.org/10.1074/jbc.M110.124636

Standard

Immobilization of the Plug Domain Inside the SecY Channel Allows Unrestricted Protein Translocation. / Lycklama a Nijeholt, Jelger A.; Bulacu, Monica; Marrink, Siewert Jan ; Driessen, Arnold J.M.

In: The Journal of Biological Chemistry, Vol. 285, No. 31, 30.07.2010, p. 23747 - 23754.

Research output: Contribution to journalArticleAcademicpeer-review

Vancouver

Lycklama a Nijeholt JA, Bulacu M, Marrink SJ, Driessen AJM. Immobilization of the Plug Domain Inside the SecY Channel Allows Unrestricted Protein Translocation. The Journal of Biological Chemistry. 2010 Jul 30;285(31):23747 - 23754. https://doi.org/10.1074/jbc.M110.124636


BibTeX

@article{5569fb9ab3af4c93bb2ed6af2dc16580,
title = "Immobilization of the Plug Domain Inside the SecY Channel Allows Unrestricted Protein Translocation",
abstract = "The SecYEG complex forms a protein-conducting channel in the inner membrane of Escherichia coli to support the translocation of secretory proteins in their unfolded state. The SecY channel is closed at the periplasmic face of the membrane by a small re-entrance loop that connects transmembrane segment 1 with 2b. This helical domain 2a is termed the plug domain. By the introduction of pairs of cysteines and crosslinkers, the plug domain was immobilized inside the channel and connected to transmembrane segment 10. Translocation was inhibited to various degrees depending on the position and crosslinker spacer length. With one of the crosslinked mutants translocation occurred unrestricted. Biochemical characterization of this mutant as well as molecular dynamics simulations suggest that only a limited movement of the plug domain suffices for translocation.",
keywords = "ESCHERICHIA-COLI, CROSS-LINKING, CONDUCTING CHANNEL, PRECURSOR PROTEINS, FORCE-FIELD, MEMBRANE, PHENOTYPES, EFFICIENT, COMPLEX, PRLA",
author = "{Lycklama a Nijeholt}, {Jelger A.} and Monica Bulacu and Marrink, {Siewert Jan} and Driessen, {Arnold J.M.}",
year = "2010",
month = jul,
day = "30",
doi = "10.1074/jbc.M110.124636",
language = "English",
volume = "285",
pages = "23747 -- 23754",
journal = "The Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC",
number = "31",

}

RIS

TY - JOUR

T1 - Immobilization of the Plug Domain Inside the SecY Channel Allows Unrestricted Protein Translocation

AU - Lycklama a Nijeholt, Jelger A.

AU - Bulacu, Monica

AU - Marrink, Siewert Jan

AU - Driessen, Arnold J.M.

PY - 2010/7/30

Y1 - 2010/7/30

N2 - The SecYEG complex forms a protein-conducting channel in the inner membrane of Escherichia coli to support the translocation of secretory proteins in their unfolded state. The SecY channel is closed at the periplasmic face of the membrane by a small re-entrance loop that connects transmembrane segment 1 with 2b. This helical domain 2a is termed the plug domain. By the introduction of pairs of cysteines and crosslinkers, the plug domain was immobilized inside the channel and connected to transmembrane segment 10. Translocation was inhibited to various degrees depending on the position and crosslinker spacer length. With one of the crosslinked mutants translocation occurred unrestricted. Biochemical characterization of this mutant as well as molecular dynamics simulations suggest that only a limited movement of the plug domain suffices for translocation.

AB - The SecYEG complex forms a protein-conducting channel in the inner membrane of Escherichia coli to support the translocation of secretory proteins in their unfolded state. The SecY channel is closed at the periplasmic face of the membrane by a small re-entrance loop that connects transmembrane segment 1 with 2b. This helical domain 2a is termed the plug domain. By the introduction of pairs of cysteines and crosslinkers, the plug domain was immobilized inside the channel and connected to transmembrane segment 10. Translocation was inhibited to various degrees depending on the position and crosslinker spacer length. With one of the crosslinked mutants translocation occurred unrestricted. Biochemical characterization of this mutant as well as molecular dynamics simulations suggest that only a limited movement of the plug domain suffices for translocation.

KW - ESCHERICHIA-COLI

KW - CROSS-LINKING

KW - CONDUCTING CHANNEL

KW - PRECURSOR PROTEINS

KW - FORCE-FIELD

KW - MEMBRANE

KW - PHENOTYPES

KW - EFFICIENT

KW - COMPLEX

KW - PRLA

U2 - 10.1074/jbc.M110.124636

DO - 10.1074/jbc.M110.124636

M3 - Article

VL - 285

SP - 23747

EP - 23754

JO - The Journal of Biological Chemistry

JF - The Journal of Biological Chemistry

SN - 0021-9258

IS - 31

ER -

ID: 1933869