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dc.contributor.authorHogrel, Gaëlle
dc.contributor.authorMarino-Puertas, Laura
dc.contributor.authorLaurent, Sébastien
dc.contributor.authorIbrahim, Ziad
dc.contributor.authorCovès, Jacques
dc.contributor.authorGirard, Eric
dc.contributor.authorGabel, Frank
dc.contributor.authorFenel, Daphna
dc.contributor.authorDaugeron, Marie-Claire
dc.contributor.authorClouet-d’Orval, Béatrice
dc.contributor.authorBasta, Tamara
dc.contributor.authorFlament, Didier
dc.contributor.authorFranzetti, Bruno
dc.identifier.citationHogrel , G , Marino-Puertas , L , Laurent , S , Ibrahim , Z , Covès , J , Girard , E , Gabel , F , Fenel , D , Daugeron , M-C , Clouet-d’Orval , B , Basta , T , Flament , D & Franzetti , B 2022 , ' Characterization of a small tRNA-binding protein that interacts with the archaeal proteasome complex ' , Molecular Microbiology , vol. 118 , no. 1-2 , pp. 16-29 .
dc.identifier.otherPURE: 279749187
dc.identifier.otherPURE UUID: ae7405e5-0a49-4f75-955d-9a7b799ca6a7
dc.identifier.otherRIS: urn:A27FB880A154C16B7A1B996321E0F399
dc.identifier.otherScopus: 85131869534
dc.descriptionAuthors acknowledge financial support from the French Agence Nationale de la Recherche (grant [ANR-18-CE11-0018-01] to B.F. and [ANR-16-CE12-0016-01] to B.C.O). This work used the platforms of the Grenoble Instruct-ERIC Centre (ISBG: UMS3518 CNRS-CEA-UGA-EMBL) with support from FRISBI (ANR-10-INBS-05-02) and GRAL, a project of the University Grenoble Alpes graduate school (Ecoles Universitaires de Recherche) CBH-EUR-GS (ANR-17-EURE-0003) within the Grenoble Partnership for Structural Biology. The IBS Electron Microscope facility is supported by the Auvergne Rhône-Alpes Region, the Fonds Feder, the Fondation pour la Recherche Médicale and GIS-IBiSA.en
dc.description.abstractThe proteasome system allows the elimination of functional or structurally impaired proteins. This includes the degradation of nascent peptides. In Archaea, how the proteasome complex interacts with the translational machinery remains to be described. Here, we characterised a small orphan protein, Q9UZY3 (Uniprot ID) conserved in Thermococcales. The protein was identified in native pull-down experiments using the proteasome regulatory complex (PAN) as bait. X-ray crystallography and SAXS experiments revealed that the protein is monomeric and adopts a β-barrel core structure with an Oligonucleotide/oligosaccharide-Binding (OB) fold, typically found in translation elongation factors. Mobility shift experiment showed that Q9UZY3 displays tRNA binding properties. Pull-downs, co-immunoprecipitation and ITC studies revealed that Q9UZY3 interacts in vitro with PAN. Native pull-downs and proteomic analysis using different versions of Q9UZY3 showed that the protein interacts with the assembled PAN-20S proteasome machinery in Pyrococcus abyssi cellular extracts. The protein was therefore named Pbp11, for Proteasome Binding Protein of 11 kDa. Interestingly, the interaction network of Pbp11 also includes ribosomal proteins, tRNA processing enzymes and exosome subunits dependent on Pbp11's N-terminal domain that was found to be essential for tRNA binding. Together these data suggest that Pbp11 participates in an interface between the proteasome and the translational machinery.
dc.relation.ispartofMolecular Microbiologyen
dc.rightsCopyright © 2022 The Authors. Molecular Microbiology published by John Wiley & Sons Ltd. This is an open access article under the terms of the Creative Commons Attribution-NonCommercial License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited and is not used for commercial purposes.en
dc.subjectRibosome-associated quality controlen
dc.subjectProtein-protein interactionen
dc.subjecttRNA bindingen
dc.subjectQH301 Biologyen
dc.subjectQH426 Geneticsen
dc.titleCharacterization of a small tRNA-binding protein that interacts with the archaeal proteasome complexen
dc.typeJournal articleen
dc.description.versionPublisher PDFen
dc.contributor.institutionUniversity of St Andrews. School of Biologyen
dc.description.statusPeer revieweden

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