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dc.contributor.authorRavichandran, KE
dc.contributor.authorKaduhr, L
dc.contributor.authorSkupien-Rabian, B
dc.contributor.authorShvetsova, E
dc.contributor.authorSokołowski, M
dc.contributor.authorKrutyhołowa, R
dc.contributor.authorKwasna, D
dc.contributor.authorBrachmann, C
dc.contributor.authorLin, S
dc.contributor.authorGuzman Perez, S
dc.contributor.authorWilk, P
dc.contributor.authorKösters, M
dc.contributor.authorGrudnik, P
dc.contributor.authorJankowska, U
dc.contributor.authorLeidel, SA
dc.contributor.authorSchaffrath, R
dc.contributor.authorGlatt, S
dc.coverage.spatialEngland
dc.date.accessioned2023-05-19T09:52:10Z
dc.date.available2023-05-19T09:52:10Z
dc.date.issued2022-10-17
dc.identifier.citationThe EMBO Journal, 2022, 41 (20), pp. e111318 -
dc.identifier.issn0261-4189
dc.identifier.urihttps://repository.icr.ac.uk/handle/internal/5790
dc.identifier.eissn1460-2075
dc.identifier.eissn1460-2075
dc.identifier.doi10.15252/embj.2022111318
dc.description.abstractPost-translational modifications by ubiquitin-like proteins (UBLs) are essential for nearly all cellular processes. Ubiquitin-related modifier 1 (Urm1) is a unique UBL, which plays a key role in tRNA anticodon thiolation as a sulfur carrier protein (SCP) and is linked to the noncanonical E1 enzyme Uba4 (ubiquitin-like protein activator 4). While Urm1 has also been observed to conjugate to target proteins like other UBLs, the molecular mechanism of its attachment remains unknown. Here, we reconstitute the covalent attachment of thiocarboxylated Urm1 to various cellular target proteins in vitro, revealing that, unlike other known UBLs, this process is E2/E3-independent and requires oxidative stress. Furthermore, we present the crystal structures of the peroxiredoxin Ahp1 before and after the covalent attachment of Urm1. Surprisingly, we show that urmylation is accompanied by the transfer of sulfur to cysteine residues in the target proteins, also known as cysteine persulfidation. Our results illustrate the role of the Uba4-Urm1 system as a key evolutionary link between prokaryotic SCPs and the UBL modifications observed in modern eukaryotes.
dc.formatPrint-Electronic
dc.format.extente111318 -
dc.languageeng
dc.language.isoeng
dc.publisherWILEY
dc.relation.ispartofThe EMBO Journal
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/
dc.subjectUrm1
dc.subjectoxidative stress
dc.subjectpersulfidation
dc.subjectsulfur transfer
dc.subjectubiquitin-like
dc.subjectAnticodon
dc.subjectCarrier Proteins
dc.subjectCysteine
dc.subjectPeroxiredoxins
dc.subjectSulfur
dc.subjectUbiquitin
dc.subjectUbiquitins
dc.titleE2/E3-independent ubiquitin-like protein conjugation by Urm1 is directly coupled to cysteine persulfidation.
dc.typeJournal Article
dcterms.dateAccepted2022-08-22
dc.date.updated2023-05-19T09:49:53Z
rioxxterms.versionVoR
rioxxterms.versionofrecord10.15252/embj.2022111318
rioxxterms.licenseref.startdate2022-10-17
rioxxterms.typeJournal Article/Review
pubs.author-urlhttps://www.ncbi.nlm.nih.gov/pubmed/36102610
pubs.issue20
pubs.organisational-group/ICR
pubs.organisational-group/ICR/Primary Group
pubs.organisational-group/ICR/Primary Group/ICR Divisions
pubs.organisational-group/ICR/Primary Group/ICR Divisions/Structural Biology
pubs.organisational-group/ICR/Primary Group/ICR Divisions/Structural Biology/Structural Biology of Cell Signalling
pubs.publication-statusPublished
pubs.publisher-urlhttp://dx.doi.org/10.15252/embj.2022111318
pubs.volume41
icr.provenanceDeposited by Mr Keerthiraju Ethiraju Ravichandran on 2023-05-19. Deposit type is initial. No. of files: 1. Files: E2E3-independent ubiquitin-like protein conjugation by Urm1 is directly coupled to cysteine persulfidation.pdf


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