DC Field | Value | Language |
---|---|---|
dc.contributor.author | Kim, Bong Heon | - |
dc.contributor.author | Kim, Min Kyung | - |
dc.contributor.author | Oh, Sun Joo | - |
dc.contributor.author | Nguyen, Kha The | - |
dc.contributor.author | Kim, Jun Hoe | - |
dc.contributor.author | Varshavsky, Alexander | - |
dc.contributor.author | Hwang, Cheol-Sang | - |
dc.contributor.author | Song, Hyun Kyu | - |
dc.date.accessioned | 2023-01-06T06:40:10Z | - |
dc.date.available | 2023-01-06T06:40:10Z | - |
dc.date.created | 2023-01-05 | - |
dc.date.issued | 2022-08 | - |
dc.identifier.issn | 0027-8424 | - |
dc.identifier.uri | https://oasis.postech.ac.kr/handle/2014.oak/114875 | - |
dc.description.abstract | <jats:p> N-degron pathways are proteolytic systems that target proteins bearing N-terminal (Nt) degradation signals (degrons) called N-degrons. Nt-Arg of a protein is among Nt-residues that can be recognized as destabilizing ones by the Arg/N-degron pathway. A proteolytic cleavage of a protein can generate Arg at the N terminus of a resulting C-terminal (Ct) fragment either directly or after Nt-arginylation of that Ct-fragment by the Ate1 arginyl-tRNA-protein transferase (R-transferase), which uses Arg-tRNA <jats:sup>Arg</jats:sup> as a cosubstrate. Ate1 can Nt-arginylate Nt-Asp, Nt-Glu, and oxidized Nt-Cys* (Cys-sulfinate or Cys-sulfonate) of proteins or short peptides. <jats:italic>Ate1</jats:italic> genes of fungi, animals, and plants have been cloned decades ago, but a three-dimensional structure of Ate1 remained unknown. A detailed mechanism of arginylation is unknown as well. We describe here the crystal structure of the Ate1 R-transferase from the budding yeast <jats:italic>Kluyveromyces lactis</jats:italic> . The 58-kDa R-transferase comprises two domains that recognize, together, an acidic Nt-residue of an acceptor substrate, the Arg residue of Arg-tRNA <jats:sup>Arg</jats:sup> , and a 3′-proximal segment of the tRNA <jats:sup>Arg</jats:sup> moiety. The enzyme’s active site is located, at least in part, between the two domains. In vitro and in vivo arginylation assays with site-directed Ate1 mutants that were suggested by structural results yielded inferences about specific binding sites of Ate1. We also analyzed the inhibition of Nt-arginylation activity of Ate1 by hemin (Fe <jats:sup>3+</jats:sup> -heme), and found that hemin induced the previously undescribed disulfide-mediated oligomerization of Ate1. Together, these results advance the understanding of R-transferase and the Arg/N-degron pathway. </jats:p> | - |
dc.language | English | - |
dc.publisher | National Academy of Sciences | - |
dc.relation.isPartOf | Proceedings of the National Academy of Sciences of the United States of America | - |
dc.title | Crystal structure of the Ate1 arginyl-tRNA-protein transferase and arginylation of N-degron substrates | - |
dc.type | Article | - |
dc.identifier.doi | 10.1073/pnas.2209597119 | - |
dc.type.rims | ART | - |
dc.identifier.bibliographicCitation | Proceedings of the National Academy of Sciences of the United States of America, v.119, no.31 | - |
dc.identifier.wosid | 000907752700017 | - |
dc.citation.number | 31 | - |
dc.citation.title | Proceedings of the National Academy of Sciences of the United States of America | - |
dc.citation.volume | 119 | - |
dc.contributor.affiliatedAuthor | Hwang, Cheol-Sang | - |
dc.identifier.scopusid | 2-s2.0-85135019336 | - |
dc.description.journalClass | 1 | - |
dc.description.journalClass | 1 | - |
dc.description.isOpenAccess | Y | - |
dc.type.docType | Article | - |
dc.subject.keywordPlus | END RULE PATHWAY | - |
dc.subject.keywordPlus | UBIQUITIN-PROTEASOME SYSTEM | - |
dc.subject.keywordPlus | TERMINAL ARGINYLATION | - |
dc.subject.keywordPlus | AMINOACYL-TRANSFER | - |
dc.subject.keywordPlus | CELLULAR-PROTEINS | - |
dc.subject.keywordPlus | ESCHERICHIA-COLI | - |
dc.subject.keywordPlus | DEGRADATION | - |
dc.subject.keywordPlus | COMPONENT | - |
dc.subject.keywordPlus | RECOGNITION | - |
dc.subject.keywordPlus | AMIDASE | - |
dc.subject.keywordAuthor | arginine | - |
dc.subject.keywordAuthor | Ate1 | - |
dc.subject.keywordAuthor | hemin | - |
dc.subject.keywordAuthor | degron | - |
dc.subject.keywordAuthor | ubiquitin | - |
dc.relation.journalWebOfScienceCategory | Multidisciplinary Sciences | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
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