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  • 2019Journal Article Overview
    [["dc.bibliographiccitation.firstpage","311"],["dc.bibliographiccitation.issue","5"],["dc.bibliographiccitation.journal","Traffic"],["dc.bibliographiccitation.lastpage","324"],["dc.bibliographiccitation.volume","20"],["dc.contributor.author","Farkas, Ákos"],["dc.contributor.author","De Laurentiis, Evelina Ines"],["dc.contributor.author","Schwappach, Blanche"],["dc.date.accessioned","2019-07-09T11:51:36Z"],["dc.date.available","2019-07-09T11:51:36Z"],["dc.date.issued","2019"],["dc.description.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 tailanchored 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 tailanchored protein targeting. Our analysis also highlights a large diversity of the ways Get3 homologs dimerize. Thus, based on the structural features of Get3 homologs, these proteins may have an unexplored functional diversity in all domains of life."],["dc.identifier.doi","10.1111/tra.12643"],["dc.identifier.pmid","30972921"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/16154"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/59973"],["dc.identifier.url","https://sfb1190.med.uni-goettingen.de/production/literature/publications/65"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.relation","SFB 1190: Transportmaschinen und Kontaktstellen zellulärer Kompartimente"],["dc.relation","SFB 1190 | P04: Der GET-Rezeptor als ein Eingangstor zum ER und sein Zusammenspiel mit GET bodies"],["dc.relation.workinggroup","RG Schwappach (Membrane Protein Biogenesis)"],["dc.rights","CC BY-NC-ND 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by-nc-nd/4.0"],["dc.subject.ddc","610"],["dc.title","The natural history of Get3‐like chaperones"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","overview_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]
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