Xenopus U3 snoRNA docks on pre-rRNA through a novel base-pairing interaction

U3 small nucleolar RNA (snoRNA) is essential for rRNA processing to form 18S ribosomal RNA (rRNA). Previously, it has been shown that nucleolin is needed to load U3 snoRNA on pre-rRNA. However, as documented here, this is not sufficient. We present data that base-pairing between the U3 hinges and th...

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Bibliographic Details
Published in:RNA (Cambridge) 2004-06, Vol.10 (6), p.942-953
Main Authors: Borovjagin, Anton V, Gerbi, Susan A
Format: Article
Language:English
Subjects:
Animals
Base Pairing
Base Sequence
Binding Sites
Evolution, Molecular
Female
In Vitro Techniques
Molecular Sequence Data
Mutation
Nucleic Acid Conformation
RNA Precursors - chemistry
RNA Precursors - genetics
RNA Precursors - metabolism
RNA Processing, Post-Transcriptional
RNA, Ribosomal, 18S - biosynthesis
RNA, Ribosomal, 18S - chemistry
RNA, Ribosomal, 18S - genetics
RNA, Small Nucleolar - chemistry
RNA, Small Nucleolar - genetics
RNA, Small Nucleolar - metabolism
Xenopus
Xenopus laevis - genetics
Xenopus laevis - metabolism
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Summary:U3 small nucleolar RNA (snoRNA) is essential for rRNA processing to form 18S ribosomal RNA (rRNA). Previously, it has been shown that nucleolin is needed to load U3 snoRNA on pre-rRNA. However, as documented here, this is not sufficient. We present data that base-pairing between the U3 hinges and the external transcribed spacer (ETS) is critical for functional alignment of U3 on its pre-rRNA substrate. Additionally, the interaction between the U3 hinges and the ETS is proposed to serve as an anchor to hold U3 on the pre-rRNA substrate, while box A at the 5' end of U3 snoRNA swivels from ETS contacts to 18S rRNA contacts. Compensatory base changes revealed base-pairing between the 3' hinge of U3 snoRNA and region E1 of the ETS in Xenopus pre-rRNA; this novel interaction is required for 18S rRNA production. In contrast, base-pairing between the 5' hinge of U3 snoRNA and region E2 of the ETS is auxiliary, unlike the case in yeast where it is required. Thus, higher and lower eukaryotes use different interactions for functional association of U3 with pre-rRNA. The U3 hinge sequence varies between species, but covariation in the ETS retains complementarity. This species-specific U3-pre-rRNA interaction offers a potential target for a new class of antibiotics to prevent ribosome biogenesis in eukaryotic pathogens.
ISSN:1355-8382
1469-9001
DOI:10.1261/rna.5256704