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dc.contributor.authorKnuppel, R.en_US
dc.contributor.authorChristensen, R.H.en_US
dc.contributor.authorGray, F.C.en_US
dc.date.accessioned2019-06-05T18:28:21Z
dc.date.available2019-06-05T18:28:21Z
dc.date.issued2018
dc.identifier.urihttps://www.scopus.com/inward/record.uri?eid=2-s2.0-85044626029&doi=10.1093%2fnar%2fgkx1236&partnerID=40&md5=d3444d36a79edd67b559c840a6bed8b8
dc.identifier.urihttp://hdl.handle.net/10713/9485
dc.description.abstractEukaryotic ribosome biogenesis is a complex dynamic process which requires the action of numerous ribosome assembly factors. Among them, the eukaryotic Rio protein family members (Rio1, Rio2 and Rio3) belong to an ancient conserved atypical protein kinase/ATPase family required for the maturation of the small ribosomal subunit (SSU). Recent structure-function analyses suggested an ATPasedependent role of the Rio proteins to regulate their dynamic association with the nascent pre-SSU. However, the evolutionary origin of this feature and the detailed molecular mechanism that allows controlled activation of the catalytic activity remained to be determined. In this work we provide functional evidence showing a conserved role of the archaeal Rio proteins for the synthesis of the SSU in archaea. Moreover, we unravel a conserved RNA-dependent regulation of the Rio ATPases, which in the case of Rio2 involves, at least, helix 30 of the SSU rRNA and the Ploop lysine within the shared RIO domain. Together, our study suggests a ribosomal RNA-mediated regulatory mechanism enabling the appropriate stimulation of Rio2 catalytic activity and subsequent release of Rio2 from the nascent pre-40S particle. Based on our findings we propose a unified release mechanism for the Rio proteins. Copyright The Author(s) 2017.en_US
dc.description.sponsorshipDepartment of Biochemistry III ‘House of the Ribosome’ and by the DFG Collaborative Research Center [SFB960- AP1] ‘Ribosome formation: principles of RNP biogenesis and control of their function’ (to S.F.-C.).; Work in the MacNeill laboratory was funded by Forskningsradet ˚ for Natur og Univers (FNU) [sagsnr. 272-05-0446]; Scottish Universities Life Sciences Alliance (SULSA); Research in the Medenbach laboratory is supported by the Bavarian Research Network for Molecular Biosystems (BioSysNet); German Research Foundation (DFG) [ME4238/1-1]; DFG Collaborative Research Center [SFB960-B11] ‘Ribosome formation: principles of RNP biogenesis and control of their function’; German Federal Ministry of Education and Research (BMBF) within the framework of the e:Med research and funding concept [01ZX1401D]; Work in the Siebers laboratory was funded by a grant from the German Science Foundation (DFG) [SI642/10-1] from the Federal Ministry of Education and Research (BMBF) [0316188A]; Work in the LaRonde laboratory was funded by National Science Foundation [MCB0953493]; Publishing of this work was supported by the German Research Foundation (DFG) within the funding program Open Access Publishing. Funding for open access charge: DFG––Open Access program.en_US
dc.description.urihttps://dx.doi.org/10.1093/nar/gkx1236en_US
dc.language.isoen-USen_US
dc.publisherOxford University Pressen_US
dc.relation.ispartofNucleic Acids Research
dc.subjectRIO proteinsen_US
dc.subjectstructure-function analysisen_US
dc.subject.meshRibosomesen_US
dc.titleInsights into the evolutionary conserved regulation of Rio ATPase activityen_US
dc.typeArticleen_US
dc.identifier.doi10.1093/nar/gkx1236


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