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

Voth, W., Schick, M., Gates, S., Li, S., Vilardi, F., Gostimskaya, I., et al. (2014). The protein targeting factor Get3 functions as ATP-independent chaperone under oxidative stress conditions. Molecular Cell, 56(1), 116-127. doi:10.1016/j.molcel.2014.08.017.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0024-46EC-5 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0028-5BC6-6
Genre: Journal Article

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 Creators:
Voth, W., Author
Schick, M., Author
Gates, S., Author
Li, S., Author
Vilardi, F., Author
Gostimskaya, I., Author
Southworth, D. R., Author
Schwappach, B.1, Author              
Jakob, U., Author
Affiliations:
1Max Planck Fellow Blanche Schwappach, ou_1548137              

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 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.

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Language(s): eng - English
 Dates: 2014-09-182014-10-02
 Publication Status: Published in print
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 Table of Contents: -
 Rev. Method: Peer
 Identifiers: DOI: 10.1016/j.molcel.2014.08.017
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Title: Molecular Cell
Source Genre: Journal
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Pages: - Volume / Issue: 56 (1) Sequence Number: - Start / End Page: 116 - 127 Identifier: -