Publication

Membrane integration of a mitochondrial signal-anchored protein does not require additional proteinaceous factors

Merklinger, E., Gofman, Y., Kedrov, A., Driessen, A. J. M., Ben-Tal, N., Shai, Y. & Rapaport, D., 1-Mar-2012, In : Biochemical Journal. 442, 2, p. 381-389 9 p.

Research output: Contribution to journalArticleAcademicpeer-review

APA

Merklinger, E., Gofman, Y., Kedrov, A., Driessen, A. J. M., Ben-Tal, N., Shai, Y., & Rapaport, D. (2012). Membrane integration of a mitochondrial signal-anchored protein does not require additional proteinaceous factors. Biochemical Journal, 442(2), 381-389. https://doi.org/10.1042/BJ20111363

Author

Merklinger, Elisa ; Gofman, Yana ; Kedrov, Alexej ; Driessen, Arnold J. M. ; Ben-Tal, Nir ; Shai, Yechiel ; Rapaport, Doron. / Membrane integration of a mitochondrial signal-anchored protein does not require additional proteinaceous factors. In: Biochemical Journal. 2012 ; Vol. 442, No. 2. pp. 381-389.

Harvard

Merklinger, E, Gofman, Y, Kedrov, A, Driessen, AJM, Ben-Tal, N, Shai, Y & Rapaport, D 2012, 'Membrane integration of a mitochondrial signal-anchored protein does not require additional proteinaceous factors', Biochemical Journal, vol. 442, no. 2, pp. 381-389. https://doi.org/10.1042/BJ20111363

Standard

Membrane integration of a mitochondrial signal-anchored protein does not require additional proteinaceous factors. / Merklinger, Elisa; Gofman, Yana; Kedrov, Alexej; Driessen, Arnold J. M.; Ben-Tal, Nir; Shai, Yechiel; Rapaport, Doron.

In: Biochemical Journal, Vol. 442, No. 2, 01.03.2012, p. 381-389.

Research output: Contribution to journalArticleAcademicpeer-review

Vancouver

Merklinger E, Gofman Y, Kedrov A, Driessen AJM, Ben-Tal N, Shai Y et al. Membrane integration of a mitochondrial signal-anchored protein does not require additional proteinaceous factors. Biochemical Journal. 2012 Mar 1;442(2):381-389. https://doi.org/10.1042/BJ20111363


BibTeX

@article{afedc712c2464ba696389fda3370c175,
title = "Membrane integration of a mitochondrial signal-anchored protein does not require additional proteinaceous factors",
abstract = "The MOM (mitochondrial outer membrane) contains SA (signal-anchored) proteins that bear at their N-terminus a single hydrophobic segment that serves as both a mitochondria] targeting signal and an anchor at the membrane. These proteins, like the vast majority of mitochondrial proteins, are encoded in the nucleus and have to be imported into the organelle. Currently, the mechanisms by which they are targeted to and inserted into the OM (outer membrane) are unclear. To shed light on these issues, we employed a recombinant version of the SA protein OM45 and a synthetic peptide corresponding to its signal-anchor segment. Both forms are associated with isolated mitochondria independently of cytosolic factors. Interaction with mitochondria was diminished when a mutated form of the signal-anchor was employed. We demonstrate that the signal-anchor peptide acquires an a-helical structure in a lipid environment and adopted a TM (transmembrane) topology within artificial lipid bilayers. Moreover, the peptide's affinity to artificial membranes with OM-like lipid composition was much higher than that of membranes with ER (endoplasmic reticulum)-like lipid composition. Collectively, our results suggest that SA proteins are specifically inserted into the MOM by a process that is not dependent on additional proteins, but is rather facilitated by the distinct lipid composition of this membrane.",
keywords = "ergosterol, mitochondrion, outer membrane, signal-anchored protein (SA protein), OUTER-MEMBRANE, PHOSPHOLIPID-BILAYERS, SACCHAROMYCES-CEREVISIAE, ANTIMICROBIAL PEPTIDES, SUBCELLULAR MEMBRANES, INSERTION PATHWAY, LIPID-COMPOSITION, TOM COMPLEX, IMPORT, HELIX",
author = "Elisa Merklinger and Yana Gofman and Alexej Kedrov and Driessen, {Arnold J. M.} and Nir Ben-Tal and Yechiel Shai and Doron Rapaport",
year = "2012",
month = mar,
day = "1",
doi = "10.1042/BJ20111363",
language = "English",
volume = "442",
pages = "381--389",
journal = "Biochemical Journal",
issn = "0264-6021",
publisher = "PORTLAND PRESS LTD",
number = "2",

}

RIS

TY - JOUR

T1 - Membrane integration of a mitochondrial signal-anchored protein does not require additional proteinaceous factors

AU - Merklinger, Elisa

AU - Gofman, Yana

AU - Kedrov, Alexej

AU - Driessen, Arnold J. M.

AU - Ben-Tal, Nir

AU - Shai, Yechiel

AU - Rapaport, Doron

PY - 2012/3/1

Y1 - 2012/3/1

N2 - The MOM (mitochondrial outer membrane) contains SA (signal-anchored) proteins that bear at their N-terminus a single hydrophobic segment that serves as both a mitochondria] targeting signal and an anchor at the membrane. These proteins, like the vast majority of mitochondrial proteins, are encoded in the nucleus and have to be imported into the organelle. Currently, the mechanisms by which they are targeted to and inserted into the OM (outer membrane) are unclear. To shed light on these issues, we employed a recombinant version of the SA protein OM45 and a synthetic peptide corresponding to its signal-anchor segment. Both forms are associated with isolated mitochondria independently of cytosolic factors. Interaction with mitochondria was diminished when a mutated form of the signal-anchor was employed. We demonstrate that the signal-anchor peptide acquires an a-helical structure in a lipid environment and adopted a TM (transmembrane) topology within artificial lipid bilayers. Moreover, the peptide's affinity to artificial membranes with OM-like lipid composition was much higher than that of membranes with ER (endoplasmic reticulum)-like lipid composition. Collectively, our results suggest that SA proteins are specifically inserted into the MOM by a process that is not dependent on additional proteins, but is rather facilitated by the distinct lipid composition of this membrane.

AB - The MOM (mitochondrial outer membrane) contains SA (signal-anchored) proteins that bear at their N-terminus a single hydrophobic segment that serves as both a mitochondria] targeting signal and an anchor at the membrane. These proteins, like the vast majority of mitochondrial proteins, are encoded in the nucleus and have to be imported into the organelle. Currently, the mechanisms by which they are targeted to and inserted into the OM (outer membrane) are unclear. To shed light on these issues, we employed a recombinant version of the SA protein OM45 and a synthetic peptide corresponding to its signal-anchor segment. Both forms are associated with isolated mitochondria independently of cytosolic factors. Interaction with mitochondria was diminished when a mutated form of the signal-anchor was employed. We demonstrate that the signal-anchor peptide acquires an a-helical structure in a lipid environment and adopted a TM (transmembrane) topology within artificial lipid bilayers. Moreover, the peptide's affinity to artificial membranes with OM-like lipid composition was much higher than that of membranes with ER (endoplasmic reticulum)-like lipid composition. Collectively, our results suggest that SA proteins are specifically inserted into the MOM by a process that is not dependent on additional proteins, but is rather facilitated by the distinct lipid composition of this membrane.

KW - ergosterol

KW - mitochondrion

KW - outer membrane

KW - signal-anchored protein (SA protein)

KW - OUTER-MEMBRANE

KW - PHOSPHOLIPID-BILAYERS

KW - SACCHAROMYCES-CEREVISIAE

KW - ANTIMICROBIAL PEPTIDES

KW - SUBCELLULAR MEMBRANES

KW - INSERTION PATHWAY

KW - LIPID-COMPOSITION

KW - TOM COMPLEX

KW - IMPORT

KW - HELIX

U2 - 10.1042/BJ20111363

DO - 10.1042/BJ20111363

M3 - Article

VL - 442

SP - 381

EP - 389

JO - Biochemical Journal

JF - Biochemical Journal

SN - 0264-6021

IS - 2

ER -

ID: 5514936