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  The natural history of Get3-like chaperones.

Farkas, A., De Larentiis, E. I., & Schwappach, B. (2019). The natural history of Get3-like chaperones. Traffic, 20(5), 311-324. doi:10.1111/tra.12643.

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Item Permalink: http://hdl.handle.net/21.11116/0000-0003-68FE-B Version Permalink: http://hdl.handle.net/21.11116/0000-0003-8966-0
Genre: Journal Article

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 Creators:
Farkas, A., Author
De Larentiis, E. I., Author
Schwappach, B.1, Author              
Affiliations:
1Max Planck Fellow Blanche Schwappach, ou_1548137              

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Free keywords: Bacteria; Chlorophyta; Embryophyta; Endoplasmic Reticulum; Get3p; Molecular Chaperone; Rhodophyta; Tail-Anchored Protein
 Abstract: Get3 in yeast or TRC40 in mammals is an ATPase that, in eukaryotes, is a central element of the GET or TRC pathway involved in the targeting of tail-anchored proteins. Get3 has also been shown to possess chaperone holdase activity. A bioinformatic assessment was performed across all domains of life on functionally important regions of Get3 including the TRC40-insert and the hydrophobic groove essential for tail-anchored protein binding. We find that such a hydrophobic groove is much more common in bacterial Get3 homologs than previously appreciated based on a directed comparison of bacterial ArsA and yeast Get3. Furthermore, our analysis shows that the region containing the TRC40-insert varies in length and methionine content to an unexpected extent within eukaryotes and also between different phylogenetic groups. In fact, since the TRC40-insert is present in all domains of life, we suggest that its presence does not automatically predict a tail-anchored protein targeting function. This opens up a new perspective on the function of organellar Get3 homologs in plants which feature the TRC40-insert but have not been demonstrated to function in tail-anchored protein targeting. Our analysis also highlights a large diversity of the ways Get3 homologs dimerize. We discuss the structural features of Get3 homologs that point to diverse functions of these proteins in all domains of life.

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Language(s): eng - English
 Dates: 2019-04-112019-05
 Publication Status: Published in print
 Pages: -
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 Table of Contents: -
 Rev. Method: Peer
 Identifiers: DOI: 10.1111/tra.12643
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Title: Traffic
Source Genre: Journal
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Pages: - Volume / Issue: 20 (5) Sequence Number: - Start / End Page: 311 - 324 Identifier: -