Two distinct yeast proteins are related to the mammalian ribosomal polypeptide L7

Lalo, Dominique; Mariotte, Sylvie; Thuriaux, Pierre

doi:10.1002/yea.320091007

Cited by 9 publications

(7 citation statements)

References 29 publications

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“…Yeast r-protein L7 shares a notable sequence similarity with the trans -acting factor Rlp7 throughout its entire primary sequence (41) (Supplementary Figure S3). Given this close homology, we could even model the predicted structure of most of the Rlp7 protein (from Lys 84 to Asn 322 ) on the basis of the structure of L7 in the crystal of yeast 60S r-subunit (19).…”

Section: Resultsmentioning

confidence: 99%

Yeast ribosomal protein L7 and its homologue Rlp7 are simultaneously present at distinct sites on pre-60S ribosomal particles

Babiano

Badis

Saveanu

et al. 2013

Nucleic Acids Research

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Ribosome biogenesis requires >300 assembly factors in Saccharomyces cerevisiae. Ribosome assembly factors Imp3, Mrt4, Rlp7 and Rlp24 have sequence similarity to ribosomal proteins S9, P0, L7 and L24, suggesting that these pre-ribosomal factors could be placeholders that prevent premature assembly of the corresponding ribosomal proteins to nascent ribosomes. However, we found L7 to be a highly specific component of Rlp7-associated complexes, revealing that the two proteins can bind simultaneously to pre-ribosomal particles. Cross-linking and cDNA analysis experiments showed that Rlp7 binds to the ITS2 region of 27S pre-rRNAs, at two sites, in helix III and in a region adjacent to the pre-rRNA processing sites C1 and E. However, L7 binds to mature 25S and 5S rRNAs and cross-linked predominantly to helix ES7Lb within 25S rRNA. Thus, despite their predicted structural similarity, our data show that Rlp7 and L7 clearly bind at different positions on the same pre-60S particles. Our results also suggest that Rlp7 facilitates the formation of the hairpin structure of ITS2 during 60S ribosomal subunit maturation.

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Section: Resultsmentioning

confidence: 99%

Yeast ribosomal protein L7 and its homologue Rlp7 are simultaneously present at distinct sites on pre-60S ribosomal particles

Babiano

Badis

Saveanu

et al. 2013

Nucleic Acids Research

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“…Triangles above the restriction map indicate the approximate positions of the rpc34-:: LUK28 (URA3), rpc34-:: LUKll (URA3), rpc34-::LUK39 (URA3) and fun34:--LUK18 (URA3) insertions. Boxes below the restriction map correspond to the rpc34-A::HIS3 (Stettler et al, 1992), rlp7-A::HIS3 (Lalo et al, 1993b), citl-A:: LEUZ (Suissa et al, 1984) and mrp7-A::URA3 (Fearon and Mason, 1988) deletions. Black boxes or triangles denote lethal alleles, whilst the dotted triangle defines the viable lac2 fusion allele fun34::LUKI8.…”

Section: Plasmids and Sequencing Strategymentioning

confidence: 99%

“…Four of the genes (RPC34, CIT1, RLP7 and MRP7) were described in previous publications (Stettler et al, 1992; *Addressee for correspondence. Suissa et al, 1984;Lalo et al, 1993b;Fearon and Mason, 1988) and will not be specifically dealt with in this paper.…”

Section: Introductionmentioning

confidence: 99%

XIV. Yeast sequencing reports. Organization of the centromeric region of chromosome XIV in Saccharomyces cerevisiae

Lalo

Stettler

Mariotte

et al. 1994

Yeast

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A 15.1 kb fragment of the yeast genome was allocated to the centromeric region of chromosome XIV by genetic mapping. It contained six bona fide genes, RPC34, FUN34, CIT1 (Suissa et al., 1984), RLP7, PET8 and MRP7 (Fearon and Mason, 1988) and two large open reading frames, DOM34 and TOM34. RPC34 and RLP7 define strictly essential functions, whereas CIT1, PET8 and MRP7 encode mitochondrial proteins. The PET8 product belongs to a family of mitochondrial carrier proteins. FUN34 encodes a putative transmembraneous protein that is non-essential as judged from the normal growth of the fun34-::LUK18(URA3) allele even on respirable substrates. TOM34 codes for a putative RNA binding protein, and DOM34 defines a hypothetical polypeptide of 35 kDa, with no significant homology to known proteins. The region under study also contains two divergently transcribed tDNAs, separated only by a chimeric transposable element. This tight tDNA linkage pattern is commonly encountered in yeast, and a general hypothesis is proposed for its emergence on the Saccharomyces cerevisiae genome. RPC34, RLP7, PET8 and MRP7 are unique on the yeast genome, but the remaining genes belong to an extant centromeric duplication between chromosome III and XIV.

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“…Therefore, we predict that Rlp7 might bind near the other A 3 factors in ITS2 or domain I to promote consecutive processing of 27SA 3 and 27SB pre-rRNAs. However, because Rlp7 shares 32% sequence identity to r-protein L7 (Lalo et al 1993;Mizuta et al 1995), it has been proposed to bind to domain II of 25S rRNA to act as a placeholder for L7 during assembly (Gadal et al 2002).…”

Section: Introductionmentioning

confidence: 99%

Identification of the binding site of Rlp7 on assembling 60S ribosomal subunits in Saccharomyces cerevisiae

Dembowski

Ramesh

McManus

et al. 2013

RNA

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Eukaryotic ribosome assembly requires over 200 assembly factors that facilitate rRNA folding, ribosomal protein binding, and prerRNA processing. One such factor is Rlp7, an essential RNA binding protein required for consecutive pre-rRNA processing steps for assembly of yeast 60S ribosomal subunits: exonucleolytic processing of 27SA 3 pre-rRNA to generate the 5 ′ end of 5.8S rRNA and endonucleolytic cleavage of the 27SB pre-rRNA to initiate removal of internal transcribed spacer 2 (ITS2). To better understand the functions of Rlp7 in 27S pre-rRNA processing steps, we identified where it crosslinks to pre-rRNA. We found that Rlp7 binds at the junction of ITS2 and the ITS2-proximal stem, between the 3 ′ end of 5.8S rRNA and the 5 ′ end of 25S rRNA. Consistent with Rlp7 binding to this neighborhood during assembly, two-hybrid and affinity copurification assays showed that Rlp7 interacts with other assembly factors that bind to or near ITS2 and the proximal stem. We used in vivo RNA structure probing to demonstrate that the proximal stem forms prior to Rlp7 binding and that Rlp7 binding induces RNA conformational changes in ITS2 that may chaperone rRNA folding and regulate 27S pre-rRNA processing. Our findings contradict the hypothesis that Rlp7 functions as a placeholder for ribosomal protein L7, from which Rlp7 is thought to have evolved in yeast. The binding site of Rlp7 is within eukaryotic-specific RNA elements, which are not found in bacteria. Thus, we propose that Rlp7 coevolved with these RNA elements to facilitate eukaryotic-specific functions in ribosome assembly and pre-rRNA processing.

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Two distinct yeast proteins are related to the mammalian ribosomal polypeptide L7

Cited by 9 publications

References 29 publications

Yeast ribosomal protein L7 and its homologue Rlp7 are simultaneously present at distinct sites on pre-60S ribosomal particles

Yeast ribosomal protein L7 and its homologue Rlp7 are simultaneously present at distinct sites on pre-60S ribosomal particles

XIV. Yeast sequencing reports. Organization of the centromeric region of chromosome XIV in Saccharomyces cerevisiae

Identification of the binding site of Rlp7 on assembling 60S ribosomal subunits in Saccharomyces cerevisiae

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