• Login
    View Item 
    •   UMB Digital Archive
    • UMB Open Access Articles
    • UMB Open Access Articles
    • View Item
    •   UMB Digital Archive
    • UMB Open Access Articles
    • UMB Open Access Articles
    • View Item
    JavaScript is disabled for your browser. Some features of this site may not work without it.

    Browse

    All of UMB Digital ArchiveCommunitiesPublication DateAuthorsTitlesSubjectsThis CollectionPublication DateAuthorsTitlesSubjects

    My Account

    LoginRegister

    Statistics

    Display statistics

    Insights into the evolutionary conserved regulation of Rio ATPase activity

    • CSV
    • RefMan
    • EndNote
    • BibTex
    • RefWorks
    Author
    Knuppel, R.
    Christensen, R.H.
    Gray, F.C.
    Date
    2018
    Journal
    Nucleic Acids Research
    Publisher
    Oxford University Press
    Type
    Article
    
    Metadata
    Show full item record
    See at
    https://dx.doi.org/10.1093/nar/gkx1236
    Abstract
    Eukaryotic 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.
    Sponsors
    Department 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.
    Keyword
    RIO proteins
    structure-function analysis
    Ribosomes
    Identifier to cite or link to this item
    https://www.scopus.com/inward/record.uri?eid=2-s2.0-85044626029&doi=10.1093%2fnar%2fgkx1236&partnerID=40&md5=d3444d36a79edd67b559c840a6bed8b8; http://hdl.handle.net/10713/9485
    ae974a485f413a2113503eed53cd6c53
    10.1093/nar/gkx1236
    Scopus Count
    Collections
    UMB Open Access Articles

    entitlement

     
    DSpace software (copyright © 2002 - 2022)  DuraSpace
    Quick Guide | Policies | Contact Us | UMB Health Sciences & Human Services Library
    Open Repository is a service operated by 
    Atmire NV
     

    Export search results

    The export option will allow you to export the current search results of the entered query to a file. Different formats are available for download. To export the items, click on the button corresponding with the preferred download format.

    By default, clicking on the export buttons will result in a download of the allowed maximum amount of items.

    To select a subset of the search results, click "Selective Export" button and make a selection of the items you want to export. The amount of items that can be exported at once is similarly restricted as the full export.

    After making a selection, click one of the export format buttons. The amount of items that will be exported is indicated in the bubble next to export format.