E2-EPF UCP possesses E3 ubiquitin ligase activity via its cysteine 118 residue

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dc.contributor.authorJung Hwa Lim-
dc.contributor.authorHee Won Shin-
dc.contributor.authorKyung-Sook Chung-
dc.contributor.authorNam-Soon Kim-
dc.contributor.authorJu Hee Kim-
dc.contributor.authorHong Ryul Jung-
dc.contributor.authorDong-Soo Im-
dc.contributor.authorCho Rok Jung-
dc.date.accessioned2017-04-19T10:26:44Z-
dc.date.available2017-04-19T10:26:44Z-
dc.date.issued2016-
dc.identifier.issn1932-6203-
dc.identifier.uri10.1371/journal.pone.0163710ko
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/13425-
dc.description.abstractHere, we show that E2-EPF ubiquitin carrier protein (UCP) elongated E3-independent polyubiquitin chains on the lysine residues of von Hippel-Lindau protein (pVHL) and its own lysine residues both in vitro and in vivo. The initiation of the ubiquitin reaction depended on not only Lys11 linkage but also the Lys6, Lys48 and Lys63 residues of ubiquitin, which were involved in polyubiquitin chain formation on UCP itself. UCP self-association occurred through the UBC domain, which also contributed to the interaction with pVHL. The polyubiquitin chains appeared on the N-terminus of UCP in vivo, which indicated that the N-terminus of UCP contains target lysines for polyubiquitination. The Lys76 residue of UCP was the most critical site for auto-ubiquitination, whereas the polyubiquitin chain formation on pVHL occurred on all three of its lysines (Lys159, Lys171 and Lys196). A UCP mutant in which Cys118 was changed to alanine (UCPC118A) did not form a polyubiquitin chain but did strongly accumulate mono- and di-ubiquitin via auto-ubiquitination. Polyubiquitin chain formation required the coordination of Cys95 and Cys118 between two interacting molecules. The mechanism of the polyubiquitin chain reaction of UCP may involve the transfer of ubiquitin from Cys95 to Cys118 by trans-thiolation, with polyubiquitin chains forming at Cys118 by reversible thioester bonding. The polyubiquitin chains are then moved to the lysine residues of the substrate by irreversible isopeptide bonding. During the elongation of the ubiquitin chain, an active Cys118 residue is required in both parts of UCP, namely, the catalytic enzyme and the substrate. In conclusion, UCP possesses not only E2 ubiquitin conjugating enzyme activity but also E3 ubiquitin ligase activity, and Cys118 is critical for polyubiquitin chain formation.-
dc.publisherPublic Library of Science-
dc.titleE2-EPF UCP possesses E3 ubiquitin ligase activity via its cysteine 118 residue-
dc.title.alternativeE2-EPF UCP possesses E3 ubiquitin ligase activity via its cysteine 118 residue-
dc.typeArticle-
dc.citation.titlePLoS One-
dc.citation.number9-
dc.citation.endPagee0163710-
dc.citation.startPagee0163710-
dc.citation.volume11-
dc.contributor.affiliatedAuthorJung Hwa Lim-
dc.contributor.affiliatedAuthorHee Won Shin-
dc.contributor.affiliatedAuthorKyung-Sook Chung-
dc.contributor.affiliatedAuthorNam-Soon Kim-
dc.contributor.affiliatedAuthorJu Hee Kim-
dc.contributor.affiliatedAuthorHong Ryul Jung-
dc.contributor.affiliatedAuthorDong-Soo Im-
dc.contributor.affiliatedAuthorCho Rok Jung-
dc.contributor.alternativeName임정화-
dc.contributor.alternativeName신희원-
dc.contributor.alternativeName정경숙-
dc.contributor.alternativeName김남순-
dc.contributor.alternativeName김주희-
dc.contributor.alternativeName정홍렬-
dc.contributor.alternativeName임동수-
dc.contributor.alternativeName정초록-
dc.identifier.bibliographicCitationPLoS One, vol. 11, no. 9, pp. e0163710-e0163710-
dc.identifier.doi10.1371/journal.pone.0163710-
dc.description.journalClassY-
Appears in Collections:
Division of Research on National Challenges > Stem Cell Convergenece Research Center > 1. Journal Articles
Division of Research on National Challenges > 1. Journal Articles
Division of Biomedical Research > Rare Disease Research Center > 1. Journal Articles
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