An in vivo and in vitro structure-function analysis of the Saccharomyces cerevisiae U3A snoRNP: protein-RNA contacts and base-pair interaction with the pre-ribosomal RNA 1 1Edited by M. Yaniv

Méreau, Agnès; Fournier, Régis; Grégoire, Anne; Mougin, Annie; Fabrizio, Patrizia; Lührmann, Reinhard; Branlant, Christiane

doi:10.1006/jmbi.1997.1320

Cited by 103 publications

(140 citation statements)

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“…Sequence analysis of U3 snoRNA reveals six evolutionarily conserved sequence elements, termed Boxes A, A′, B, C, C′ and D (17)(18)(19)(20)(21)(22)(23)(24)(25)(26)(27). Boxes A and A′ are located in the 5′ domain of U3 snoRNA and, along with the 'hinge' region, base pair to sites within the pre-rRNA to direct the multiple endonucleolytic cleavages necessary for the maturation of 18S rRNA (15,16,23,25,28). Boxes B, C, C′ and D are found in the 3′ domain of U3 and have been characterized as sequences required for protein association (17,19,23,25,29).…”

Section: Introductionmentioning

confidence: 99%

“…Boxes A and A′ are located in the 5′ domain of U3 snoRNA and, along with the 'hinge' region, base pair to sites within the pre-rRNA to direct the multiple endonucleolytic cleavages necessary for the maturation of 18S rRNA (15,16,23,25,28). Boxes B, C, C′ and D are found in the 3′ domain of U3 and have been characterized as sequences required for protein association (17,19,23,25,29). The secondary structure of the 3′ domain positions Boxes B and C, as well as Boxes C′ and D into discrete loops flanked by base paired stems to form the Box B/C and Box C′/D motifs, respectively (23,27,30).…”

Section: Introductionmentioning

confidence: 99%

“…Boxes B, C, C′ and D are found in the 3′ domain of U3 and have been characterized as sequences required for protein association (17,19,23,25,29). The secondary structure of the 3′ domain positions Boxes B and C, as well as Boxes C′ and D into discrete loops flanked by base paired stems to form the Box B/C and Box C′/D motifs, respectively (23,27,30). The Box C′/D motif of U3 is equivalent to the Box C/D motifs of other members of this snoRNA family in sequence/structure and function (23,27,30).…”

Section: Introductionmentioning

confidence: 99%

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Interaction of the U3-55k protein with U3 snoRNA is mediated by the Box B/C motif of U3 and the WD repeats of U3-55k

Lukowiak

Granneman²,

Mattox

et al. 2000

Nucleic Acids Research

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U3 small nucleolar RNA (snoRNA) is a member of the Box C/D family of snoRNAs which functions in ribosomal RNA processing. U3-55k is a protein that has been found to interact with U3 but not other members of the Box C/D snoRNA family. We have found that interaction of the U3-55k protein with U3 RNA in vivo is mediated by the conserved Box B/C motif which is unique to U3 snoRNA. Mutation of Box B and Box C, but not of other conserved sequence elements, disrupted interaction of U3-55k with U3 RNA. Furthermore, a fragment of U3 containing only these two conserved elements was bound by U3-55k in vivo. RNA binding assays performed in vitro indicate that Box C may be the primary determinant of the interaction. We have cloned the cDNA encoding the Xenopus laevis U3-55k protein and find strong homology to the human sequence, including six WD repeats. Deletion of WD repeats or sequences near the C-terminus of U3-55k resulted in loss of association with U3 RNA and also loss of localization of U3-55k to the nucleolus, suggesting that protein-protein interactions contribute to the localization and RNA binding of U3-55k in vivo.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Interaction of the U3-55k protein with U3 snoRNA is mediated by the Box B/C motif of U3 and the WD repeats of U3-55k

Lukowiak

Granneman²,

Mattox

et al. 2000

Nucleic Acids Research

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“…This chaperone-like function of U3 has been supported by results of chemical modification (Méreau et al 1997) and compensatory base changes (Sharma and Tollervey 1999) in yeast. Our data from Xenopus suggest that the base-pairing between the U3 hinges and the ETS may be required to position U3 boxes AЈ and A for base-pairing with the18S stem-loop and possibly even other downstream regions in pre-rRNA .…”

Section: Correct Placement Of U3 Snorna On Pre-rrna For Rrna Processimentioning

confidence: 72%

“…What keeps U3 snoRNA inactive after it has docked on the nascent pre-rRNA? The GAC element, box AЈ and box A are required for 18S rRNA production in Xenopus , apparently through base-pairing interactions with the 18S region of pre-rRNA (Hughes 1996;Méreau et al 1997;Sharma and Tollervey 1999;Borovjagin and Gerbi 2001). However, intramolecular base-pairing of these sequences within U3 domain I (Fig.…”

Section: Inactivity Of U3 Snorna Until Transcription Is Completedmentioning

confidence: 99%

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

Borovjagin

Gerbi²

2004

RNA

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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.

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