Structure of the ArgRS-GlnRS-AIMP1 complex and its implications for mammalian translation

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dc.contributor.authorY Fu-
dc.contributor.authorY Kim-
dc.contributor.authorK S Jin-
dc.contributor.authorH S Kim-
dc.contributor.authorJ H Kim-
dc.contributor.authorD M Wang-
dc.contributor.authorM Park-
dc.contributor.authorC H Jo-
dc.contributor.authorN H Kwon-
dc.contributor.authorD Kim-
dc.contributor.authorMyung Hee Kim-
dc.contributor.authorY H Jeon-
dc.contributor.authorK Y Hwang-
dc.contributor.authorS Kim-
dc.contributor.authorY Cho-
dc.date.accessioned2017-04-19T09:57:53Z-
dc.date.available2017-04-19T09:57:53Z-
dc.date.issued2014-
dc.identifier.issn0027-8424-
dc.identifier.uri10.1073/pnas.1408836111ko
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/12253-
dc.description.abstractIn higher eukaryotes, one of the two arginyl-tRNA synthetases (ArgRSs) has evolved to have an extended N-terminal domain that plays a crucial role in protein synthesis and cell growth and in integration into the multisynthetase complex (MSC). Here, we report a crystal structure of the MSC subcomplex comprising ArgRS, glutaminyl-tRNA synthetase (GlnRS), and the auxiliary factor aminoacyl tRNA synthetase complex-interacting multifunctional protein 1 (AIMP1)/p43. In this complex, the N-terminal domain of ArgRS forms a long coiled-coil structure with the N-terminal helix of AIMP1 and anchors the C-terminal core of GlnRS, thereby playing a central role in assembly of the three components. Mutation of AIMP1 destabilized the N-terminal helix of ArgRS and abrogated its catalytic activity. Mutation of the N-terminal helix of ArgRS liberated GlnRS, which is known to control cell death. This ternary complex was further anchored to AIMP2/p38 through interaction with AIMP1. These findings demonstrate the importance of interactions between the N-terminal domains of ArgRS and AIMP1 for the catalytic and noncatalytic activities of ArgRS and for the assembly of the higher-order MSC protein complex.-
dc.publisherNatl Acad Sciences-
dc.titleStructure of the ArgRS-GlnRS-AIMP1 complex and its implications for mammalian translation-
dc.title.alternativeStructure of the ArgRS-GlnRS-AIMP1 complex and its implications for mammalian translation-
dc.typeArticle-
dc.citation.titleProceedings of National Academy of Sciences of United States of America-
dc.citation.number42-
dc.citation.endPage15089-
dc.citation.startPage15084-
dc.citation.volume111-
dc.contributor.affiliatedAuthorMyung Hee Kim-
dc.contributor.alternativeNameFu-
dc.contributor.alternativeName김영란-
dc.contributor.alternativeName진경식-
dc.contributor.alternativeName김현숙-
dc.contributor.alternativeName김종현-
dc.contributor.alternativeNameWang-
dc.contributor.alternativeName박민영-
dc.contributor.alternativeName조창화-
dc.contributor.alternativeName권남훈-
dc.contributor.alternativeName김도연-
dc.contributor.alternativeName김명희-
dc.contributor.alternativeName전영호-
dc.contributor.alternativeName황광연-
dc.contributor.alternativeName김성훈-
dc.contributor.alternativeName조윤제-
dc.identifier.bibliographicCitationProceedings of National Academy of Sciences of United States of America, vol. 111, no. 42, pp. 15084-15089-
dc.identifier.doi10.1073/pnas.1408836111-
dc.subject.keywordAIMP1-
dc.subject.keywordArginyl-tRNA synthetase-
dc.subject.keywordCrystal structure-
dc.subject.keywordGlutaminyl-tRNA synthetase-
dc.subject.keywordMultisynthetase complex-
dc.subject.localAIMP1-
dc.subject.localArginyl-tRNA synthetase-
dc.subject.localcrystal structure-
dc.subject.localCrystal structure-
dc.subject.localGlutaminyl-tRNA synthetase-
dc.subject.localMultisynthetase complex-
dc.description.journalClassY-
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Division of Biomedical Research > Microbiome Convergence Research Center > 1. Journal Articles
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