Solution structure of MUL1-RING domain and its interaction with p53 transactivation domain

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dc.contributor.authorMin-Sung Lee-
dc.contributor.authorSang-Ok Lee-
dc.contributor.authorMi-Kyung Lee-
dc.contributor.authorG S Yi-
dc.contributor.authorC K Lee-
dc.contributor.authorK S Ryu-
dc.contributor.authorSeung-Wook Chi-
dc.date.accessioned2019-10-28T16:30:27Z-
dc.date.available2019-10-28T16:30:27Z-
dc.date.issued2019-
dc.identifier.issn0006-291X-
dc.identifier.uri10.1016/j.bbrc.2019.06.101ko
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/18948-
dc.description.abstractMitochondrial E3 ubiquitin ligase 1 (MUL1) is a multifunctional mitochondrial protein involved in various biological processes such as mitochondrial dynamics, cell growth, apoptosis, and mitophagy. MUL1 mediates the ubiquitylation of mitochondrial p53 for proteasomal degradation. Although the interaction of MUL1-RING domain with its substrate, p53, is a unique mechanism in RING-mediated ubiquitylation, the molecular basis of this process remains unknown. In this study, we determined the solution structure of the MUL1-RING domain and characterized its interaction with the p53 transactivation domain (p53-TAD) by nuclear magnetic resonance (NMR) spectroscopy. The overall structure of the MUL1-RING domain is similar to those of RING domains of other E3 ubiquitinases. The MUL1-RING domain adopts a ββαβ fold with three anti-parallel β-strands and one α-helix, containing a canonical cross-brace motif for the ligation of two zinc ions. Through NMR chemical shift perturbation experiments, we determined the p53-TAD-binding site in the MUL1-RING domain and showed that the MUL1-RING domain interacts mainly with the p53-TAD2 subdomain composed of residues 39-57. Taken together, our results provide a molecular basis for the novel recognition mechanism of the p53-TAD substrate by the MUL1-RING domain.-
dc.publisherElsevier-
dc.titleSolution structure of MUL1-RING domain and its interaction with p53 transactivation domain-
dc.title.alternativeSolution structure of MUL1-RING domain and its interaction with p53 transactivation domain-
dc.typeArticle-
dc.citation.titleBiochemical and Biophysical Research Communications-
dc.citation.number0-
dc.citation.endPage539-
dc.citation.startPage533-
dc.citation.volume516-
dc.contributor.affiliatedAuthorMin-Sung Lee-
dc.contributor.affiliatedAuthorSang-Ok Lee-
dc.contributor.affiliatedAuthorMi-Kyung Lee-
dc.contributor.affiliatedAuthorSeung-Wook Chi-
dc.contributor.alternativeName이민성-
dc.contributor.alternativeName이상옥-
dc.contributor.alternativeName이미경-
dc.contributor.alternativeName이관수-
dc.contributor.alternativeName이종길-
dc.contributor.alternativeName류경석-
dc.contributor.alternativeName지승욱-
dc.identifier.bibliographicCitationBiochemical and Biophysical Research Communications, vol. 516, pp. 533-539-
dc.identifier.doi10.1016/j.bbrc.2019.06.101-
dc.subject.keywordMitochondrial E3 ubiquitin ligase 1-
dc.subject.keywordProtein-protein interaction-
dc.subject.keywordRING domain-
dc.subject.keywordSolution structure-
dc.subject.keywordTransactivation domain-
dc.subject.keywordp53-
dc.subject.localmitochondrial E3 ubiquitin ligase 1-
dc.subject.localMitochondrial E3 ubiquitin ligase 1-
dc.subject.localProtein-protein interaction-
dc.subject.localProteinprotein interactions-
dc.subject.localProtein-Protein Interaction-
dc.subject.localProtein-Protein interaction-
dc.subject.localprotein-protein interaction-
dc.subject.localProtein-protein interactions-
dc.subject.localRING domain-
dc.subject.localSolution structure-
dc.subject.localsolution structure-
dc.subject.localTransactivation domain-
dc.subject.localtransactivation domain-
dc.subject.localP53-
dc.subject.localp53-
dc.description.journalClassY-
Appears in Collections:
Critical Diseases Diagnostics Convergence Research Center > 1. Journal Articles
Division of Biomedical Research > 1. Journal Articles
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