Hostname: page-component-586b7cd67f-dsjbd Total loading time: 0 Render date: 2024-11-24T07:56:26.567Z Has data issue: false hasContentIssue false

p62, a novel Xenopus laevis component of box C/D snoRNPs

Published online by Cambridge University Press:  01 March 2000

DANIELA FILIPPINI
Affiliation:
Dipartimento di Genetica e Biologia Molecolare, Istituto Pasteur Fondazione Cenci-Bolognetti, Universitá “La Sapienza,” Rome, Italy
IRENE BOZZONI
Affiliation:
Dipartimento di Genetica e Biologia Molecolare, Istituto Pasteur Fondazione Cenci-Bolognetti, Universitá “La Sapienza,” Rome, Italy
ELISA CAFFARELLI
Affiliation:
Centro Acidi Nucleici of Consiglio Nazionale delle Richerche, Rome, Italy
Get access

Abstract

U16 belongs to the family of box C/D small nucleolar RNAs (snoRNAs) whose members participate in ribosome biogenesis, mainly acting as guides for site-specific methylation of the pre-rRNA. Like all the other members of the family, U16 is associated with a set of protein factors forming a ribonucleoprotein particle, localized in the nucleolus. So far, only a few box C/D-specific proteins are known: in Xenopus laevis, fibrillarin and p68 have been identified by UV crosslinking and shown to require the conserved boxes C and D for snoRNA interaction. In this study, we have identified an additional protein factor (p62), common to box C/D snoRNPs, that crosslinks to the internal stem region, distinct from the conserved box C/D “core motif,” of U16 snoRNA. We show here that, although the absence of the core motif and, as a consequence, of fibrillarin and p68 binding prevents processing and accumulation of the snoRNA, the lack of the internal stem does not interfere with the efficient release of U16 from its host intron and only slightly affects snoRNA stability. Because this region is likely to be the binding site for p62, we propose that this protein plays an accessory role in the formation of a mature and stable U16 snoRNP particle.

Type
Research Article
Copyright
2000 RNA Society

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)