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The protein targeting factor Get3 functions as ATP-independent chaperone under oxidative stress conditions

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The protein targeting factor Get3 functions as ATP-independent chaperone under oxidative stress conditions. / Voth, Wilhelm; Schick, Markus; Gates, Stephanie; Li, Sheng; Vilardi, Fabio; Gostimskaya, Irina; Southworth, Daniel R; Schwappach, Blanche; Jakob, Ursula.

In: MOL CELL, Vol. 56, No. 1, 02.10.2014, p. 116-27.

Research output: SCORING: Contribution to journal › SCORING: Journal article › Research › peer-review

Harvard

Voth, W, Schick, M, Gates, S, Li, S, Vilardi, F, Gostimskaya, I, Southworth, DR, Schwappach, B & Jakob, U 2014, 'The protein targeting factor Get3 functions as ATP-independent chaperone under oxidative stress conditions', MOL CELL, vol. 56, no. 1, pp. 116-27. https://doi.org/10.1016/j.molcel.2014.08.017

APA

Voth, W., Schick, M., Gates, S., Li, S., Vilardi, F., Gostimskaya, I., Southworth, D. R., Schwappach, B., & Jakob, U. (2014). The protein targeting factor Get3 functions as ATP-independent chaperone under oxidative stress conditions. MOL CELL, 56(1), 116-27. https://doi.org/10.1016/j.molcel.2014.08.017

Vancouver

Voth W, Schick M, Gates S, Li S, Vilardi F, Gostimskaya I et al. The protein targeting factor Get3 functions as ATP-independent chaperone under oxidative stress conditions. MOL CELL. 2014 Oct 2;56(1):116-27. https://doi.org/10.1016/j.molcel.2014.08.017

Bibtex

@article{dbdc67ee3b6f405f8f10b0a9b5fb3529,
title = "The protein targeting factor Get3 functions as ATP-independent chaperone under oxidative stress conditions",
abstract = "Exposure of cells to reactive oxygen species (ROS) causes a rapid and significant drop in intracellular ATP levels. This energy depletion negatively affects ATP-dependent chaperone systems, making ROS-mediated protein unfolding and aggregation a potentially very challenging problem. Here we show that Get3, a protein involved in ATP-dependent targeting of tail-anchored (TA) proteins under nonstress conditions, turns into an effective ATP-independent chaperone when oxidized. Activation of Get3's chaperone function, which is a fully reversible process, involves disulfide bond formation, metal release, and its conversion into distinct, higher oligomeric structures. Mutational studies demonstrate that the chaperone activity of Get3 is functionally distinct from and likely mutually exclusive with its targeting function, and responsible for the oxidative stress-sensitive phenotype that has long been noted for yeast cells lacking functional Get3. These results provide convincing evidence that Get3 functions as a redox-regulated chaperone, effectively protecting eukaryotic cells against oxidative protein damage.",
keywords = "Adenosine Triphosphatases/chemistry, Adenosine Triphosphate/metabolism, Guanine Nucleotide Exchange Factors/chemistry, Models, Biological, Molecular Chaperones/metabolism, Oxidation-Reduction, Oxidative Stress, Protein Unfolding, Saccharomyces cerevisiae/metabolism, Saccharomyces cerevisiae Proteins/chemistry",
author = "Wilhelm Voth and Markus Schick and Stephanie Gates and Sheng Li and Fabio Vilardi and Irina Gostimskaya and Southworth, {Daniel R} and Blanche Schwappach and Ursula Jakob",
note = "Copyright {\textcopyright} 2014 Elsevier Inc. All rights reserved.",
year = "2014",
month = oct,
day = "2",
doi = "10.1016/j.molcel.2014.08.017",
language = "English",
volume = "56",
pages = "116--27",
journal = "MOL CELL",
issn = "1097-2765",
publisher = "Cell Press",
number = "1",

}

RIS

TY - JOUR

T1 - The protein targeting factor Get3 functions as ATP-independent chaperone under oxidative stress conditions

AU - Voth, Wilhelm

AU - Schick, Markus

AU - Gates, Stephanie

AU - Li, Sheng

AU - Vilardi, Fabio

AU - Gostimskaya, Irina

AU - Southworth, Daniel R

AU - Schwappach, Blanche

AU - Jakob, Ursula

N1 - Copyright © 2014 Elsevier Inc. All rights reserved.

PY - 2014/10/2

Y1 - 2014/10/2

N2 - Exposure of cells to reactive oxygen species (ROS) causes a rapid and significant drop in intracellular ATP levels. This energy depletion negatively affects ATP-dependent chaperone systems, making ROS-mediated protein unfolding and aggregation a potentially very challenging problem. Here we show that Get3, a protein involved in ATP-dependent targeting of tail-anchored (TA) proteins under nonstress conditions, turns into an effective ATP-independent chaperone when oxidized. Activation of Get3's chaperone function, which is a fully reversible process, involves disulfide bond formation, metal release, and its conversion into distinct, higher oligomeric structures. Mutational studies demonstrate that the chaperone activity of Get3 is functionally distinct from and likely mutually exclusive with its targeting function, and responsible for the oxidative stress-sensitive phenotype that has long been noted for yeast cells lacking functional Get3. These results provide convincing evidence that Get3 functions as a redox-regulated chaperone, effectively protecting eukaryotic cells against oxidative protein damage.

AB - Exposure of cells to reactive oxygen species (ROS) causes a rapid and significant drop in intracellular ATP levels. This energy depletion negatively affects ATP-dependent chaperone systems, making ROS-mediated protein unfolding and aggregation a potentially very challenging problem. Here we show that Get3, a protein involved in ATP-dependent targeting of tail-anchored (TA) proteins under nonstress conditions, turns into an effective ATP-independent chaperone when oxidized. Activation of Get3's chaperone function, which is a fully reversible process, involves disulfide bond formation, metal release, and its conversion into distinct, higher oligomeric structures. Mutational studies demonstrate that the chaperone activity of Get3 is functionally distinct from and likely mutually exclusive with its targeting function, and responsible for the oxidative stress-sensitive phenotype that has long been noted for yeast cells lacking functional Get3. These results provide convincing evidence that Get3 functions as a redox-regulated chaperone, effectively protecting eukaryotic cells against oxidative protein damage.

KW - Adenosine Triphosphatases/chemistry

KW - Adenosine Triphosphate/metabolism

KW - Guanine Nucleotide Exchange Factors/chemistry

KW - Models, Biological

KW - Molecular Chaperones/metabolism

KW - Oxidation-Reduction

KW - Oxidative Stress

KW - Protein Unfolding

KW - Saccharomyces cerevisiae/metabolism

KW - Saccharomyces cerevisiae Proteins/chemistry

U2 - 10.1016/j.molcel.2014.08.017

DO - 10.1016/j.molcel.2014.08.017

M3 - SCORING: Journal article

C2 - 25242142

VL - 56

SP - 116

EP - 127

JO - MOL CELL

JF - MOL CELL

SN - 1097-2765

IS - 1

ER -