Date
2021-09-09Author
Kaduhr, LarsBrachmann, CindyEthiraju Ravichandran, KeerthirajuWest, James D.Glatt, SebastianSchaffrath, RaffaelSubject
570 Life sciences; biology Saccharomyces cerevisiaeUbiquitin-ähnliche ProteinePeroxiredoxinTransfer-RNSMetadata
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Aufsatz
Urm1, not quite a ubiquitin-like modifier?
Abstract
Ubiquitin related modifier 1 (Urm1) is a unique eukaryotic member of the ubiquitin-fold (UbF) protein family and conserved from yeast to humans. Urm1 is dual-functional, acting both as a sulfur carrier for thiolation of tRNA anticodons and as a protein modifier in a lysine-directed Ub-like conjugation also known as urmylation. Although Urm1 conjugation coincides with oxidative stress and targets proteins like 2-Cys peroxiredoxins from yeast (Ahp1) and fly (Prx5), it was unclear how urmylation proceeds molecularly and whether it is affected by the activity of these antioxidant enzymes. An in-depth study of Ahp1 urmylation in yeast from our laboratory (Brachmann et al., 2020) uncovered that promiscuous lysine target sites and specific redox requirements determine the Urm1 acceptor activity of the peroxiredoxin. The results clearly show that the dimer interface and the 2-Cys based redox-active centers of Ahp1 are affecting the Urm1 conjugation reaction. Together with in vivo assays demonstrating that high organic peroxide concentrations can prevent Ahp1 from being urmylated, Brachmann et al. provide insights into a potential link between Urm1 utilization and oxidant defense of cells. Here, we highlight these major findings and discuss wider implications with regards to an emerging link between Urm1 conjugation and redox biology. Moreover, from these studies we propose to redefine our perspective on Urm1 and the molecular nature of urmylation, a post-translational conjugation that may not be that ubiquitin-like after all.
Citation
In: Microbial Cell Volume 8 / No. 11 (2021-09-09) , S. 256-261 ; eissn:2311-2638Sponsorship
Gefördert durch den Publikationsfonds der Universität KasselCitation
@article{doi:10.17170/kobra-202112175278,
author={Kaduhr, Lars and Brachmann, Cindy and Ethiraju Ravichandran, Keerthiraju and West, James D. and Glatt, Sebastian and Schaffrath, Raffael},
title={Urm1, not quite a ubiquitin-like modifier?},
journal={Microbial Cell},
year={2021}
}
0500 Oax 0501 Text $btxt$2rdacontent 0502 Computermedien $bc$2rdacarrier 1100 2021$n2021 1500 1/eng 2050 ##0##http://hdl.handle.net/123456789/13448 3000 Kaduhr, Lars 3010 Brachmann, Cindy 3010 Ethiraju Ravichandran, Keerthiraju 3010 West, James D. 3010 Glatt, Sebastian 3010 Schaffrath, Raffael 4000 Urm1, not quite a ubiquitin-like modifier? / Kaduhr, Lars 4030 4060 Online-Ressource 4085 ##0##=u http://nbn-resolving.de/http://hdl.handle.net/123456789/13448=x R 4204 \$dAufsatz 4170 5550 {{Saccharomyces cerevisiae}} 5550 {{Ubiquitin-ähnliche Proteine}} 5550 {{Peroxiredoxin}} 5550 {{Transfer-RNS}} 7136 ##0##http://hdl.handle.net/123456789/13448
2021-12-20T16:33:15Z 2021-12-20T16:33:15Z 2021-09-09 doi:10.17170/kobra-202112175278 http://hdl.handle.net/123456789/13448 Gefördert durch den Publikationsfonds der Universität Kassel eng Namensnennung 4.0 International http://creativecommons.org/licenses/by/4.0/ yeast Urm1 peroxiredoxin Ahp1 protein urmylation tRNA thiolation 570 Urm1, not quite a ubiquitin-like modifier? Aufsatz Ubiquitin related modifier 1 (Urm1) is a unique eukaryotic member of the ubiquitin-fold (UbF) protein family and conserved from yeast to humans. Urm1 is dual-functional, acting both as a sulfur carrier for thiolation of tRNA anticodons and as a protein modifier in a lysine-directed Ub-like conjugation also known as urmylation. Although Urm1 conjugation coincides with oxidative stress and targets proteins like 2-Cys peroxiredoxins from yeast (Ahp1) and fly (Prx5), it was unclear how urmylation proceeds molecularly and whether it is affected by the activity of these antioxidant enzymes. An in-depth study of Ahp1 urmylation in yeast from our laboratory (Brachmann et al., 2020) uncovered that promiscuous lysine target sites and specific redox requirements determine the Urm1 acceptor activity of the peroxiredoxin. The results clearly show that the dimer interface and the 2-Cys based redox-active centers of Ahp1 are affecting the Urm1 conjugation reaction. Together with in vivo assays demonstrating that high organic peroxide concentrations can prevent Ahp1 from being urmylated, Brachmann et al. provide insights into a potential link between Urm1 utilization and oxidant defense of cells. Here, we highlight these major findings and discuss wider implications with regards to an emerging link between Urm1 conjugation and redox biology. Moreover, from these studies we propose to redefine our perspective on Urm1 and the molecular nature of urmylation, a post-translational conjugation that may not be that ubiquitin-like after all. open access Kaduhr, Lars Brachmann, Cindy Ethiraju Ravichandran, Keerthiraju West, James D. Glatt, Sebastian Schaffrath, Raffael doi:10.15698/mic2021.11.763 Saccharomyces cerevisiae Ubiquitin-ähnliche Proteine Peroxiredoxin Transfer-RNS publishedVersion eissn:2311-2638 No. 11 Microbial Cell 256-261 Volume 8 false
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