title: Chaperoning 5S RNA assembly.
abstract: In eukaryotes, three of the four ribosomal RNAs (rRNAs)—the 5.8S, 18S, and 25S/28S rRNAs—are processed from a single pre-rRNA transcript and assembled into ribosomes. The fourth rRNA, the 5S rRNA, is transcribed by RNA polymerase III and is assembled into the 5S ribonucleoprotein particle (RNP), containing ribosomal proteins Rpl5/uL18 and Rpl11/uL5, prior to its incorporation into preribosomes. In mammals, the 5S RNP is also a central regulator of the homeostasis of the tumor suppressor p53. The nucleolar localization of the 5S RNP and its assembly into preribosomes are performed by a specialized complex composed of Rpf2 and Rrs1 in yeast or Bxdc1 and hRrs1 in humans. Here we report the structural and functional characterization of the Rpf2-Rrs1 complex alone, in complex with the 5S RNA, and within pre-60S ribosomes. We show that the Rpf2-Rrs1 complex contains a specialized 5S RNA E-loop-binding module, contacts the Rpl5 protein, and also contacts the ribosome assembly factor Rsa4 and the 25S RNA. We propose that the Rpf2-Rrs1 complex establishes a network of interactions that guide the incorporation of the 5S RNP in preribosomes in the initial conformation prior to its rotation to form the central protuberance found in the mature large ribosomal subunit.
authors.affiliation: Laboratoire de Cristallographie et RMN Biologiques, UMR, CNRS 8015, Université Paris Descartes, Faculté de Pharmacie, Sorbonne Paris Cité, 75006 Paris, France;
authors.forename: Clément
authors.initials: C
authors.lastname: Madru
authors.affiliation: Laboratoire de Cristallographie et RMN Biologiques, UMR, CNRS 8015, Université Paris Descartes, Faculté de Pharmacie, Sorbonne Paris Cité, 75006 Paris, France; CR2 INSERM;
authors.forename: Simon
authors.initials: S
authors.lastname: Lebaron
authors.affiliation: Laboratoire de Cristallographie et RMN Biologiques, UMR, CNRS 8015, Université Paris Descartes, Faculté de Pharmacie, Sorbonne Paris Cité, 75006 Paris, France;
authors.forename: Magali
authors.initials: M
authors.lastname: Blaud
authors.affiliation: Laboratoire de Cristallographie et RMN Biologiques, UMR, CNRS 8015, Université Paris Descartes, Faculté de Pharmacie, Sorbonne Paris Cité, 75006 Paris, France;
authors.forename: Lila
authors.initials: L
authors.lastname: Delbos
authors.affiliation: Plateforme Génomique, Institut Cochin, UMR_S1016, INSERM, 75006 Paris, France;
authors.forename: Juliana
authors.initials: J
authors.lastname: Pipoli
authors.affiliation: Service de Biochimie et Génétique Moléculaire, Hôpital Cochin, Assistance Publique-Hôpitaux de Paris, 75006 Paris, France.
authors.forename: Eric
authors.initials: E
authors.lastname: Pasmant
authors.affiliation: Laboratoire de Cristallographie et RMN Biologiques, UMR, CNRS 8015, Université Paris Descartes, Faculté de Pharmacie, Sorbonne Paris Cité, 75006 Paris, France;
authors.forename: Stéphane
authors.initials: S
authors.lastname: Réty
authors.affiliation: Laboratoire de Cristallographie et RMN Biologiques, UMR, CNRS 8015, Université Paris Descartes, Faculté de Pharmacie, Sorbonne Paris Cité, 75006 Paris, France;
authors.forename: Nicolas
authors.initials: N
authors.lastname: Leulliot
mesh_terms: D001665:Binding Sites; D020285:Cryoelectron Microscopy; D008958:Models, Molecular; D009687:Nuclear Proteins / Q000737:chemistry* / Q000378:metabolism; D011485:Protein Binding; D020836:Protein Structure, Quaternary; D012341:RNA, Ribosomal, 5S / Q000737:chemistry / Q000378:metabolism*; D016601:RNA-Binding Proteins / Q000737:chemistry* / Q000378:metabolism; D012441:Saccharomyces cerevisiae / Q000737:chemistry / Q000378:metabolism; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry* / Q000378:metabolism
chemical_list: D009687:Nuclear Proteins; D012341:RNA, Ribosomal, 5S; D016601:RNA-Binding Proteins; C451023:RPF2 protein, S cerevisiae; C485770:RRS1 protein, S cerevisiae; D029701:Saccharomyces cerevisiae Proteins
keywords: 5S RNP; Brix domain; p53; ribosome assembly