A new rRNA processing mutant of<i>Saccharomyces cerevisiae</i>

Lindahl, Lasse; Archer, Richard; Zengel, Janice M.

doi:10.1093/nar/20.2.295

Cited by 70 publications

(100 citation statements)

References 31 publications

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“…In addition, a 5' extended form of 5.8S rRNA accumulates in the A3A1O mutant, the hybridization pattern and gel mobility of which are consistent with its extending from the 3' end of 5.8S rRNA to site A2. It is possible that this RNA is protected from further processing by being assembled into ribosomal subunits and transported to the cytoplasm, as is reported to occur in mutants in RNase MRP (Shuai and Warner, 1991;Lindahl et al, 1992;Chu et al, 1993;Schmitt and Clayton, 1993).…”

Section: Analysis Of the Effects Of Large Deletions In Its1mentioning

confidence: 95%

The 5′ end of yeast 5.8S rRNA is generated by exonucleases from an upstream cleavage site.

et al. 1994

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We have developed techniques for the detailed analysis of cis-acting sequences in the pre-rRNA of Saccharomyces cerevisiae and used these to study the processing of internal transcribed spacer 1 (ITS1) leading to the synthesis of 5.8S rRNA. As is the case for many eukaryotes, the 5' end of yeast 5.8S rRNA is heterogeneous; we designate the major, short form 5.8S(S), and the minor form (which is seven or eight nucleotides longer) 5.8S(L). These RNAs do not have a precursor/product relationship, but result from the use of alternative processing pathways. In the major pathway, a previously unidentified processing site in ITS1, designated A3, is cleaved. A 10 nucleotide deletion at site A3 strongly inhibits processing of A3 and the synthesis of 5.8S(S); processing is predominantly transferred to the alternative 5.8S(L) pathway. Site A3 lies 76 nucleotides 5' to the end of 5.8S(S), and acts as an entry site for 5'-3' exonuclease digestion which generates the 5' end of 5.8S(S). This pathway is inhibited in strains mutant for XRNlp and RATlp. Both of these proteins have been reported to have 5'-3' exonuclease activity in vitro. Formation of 5.8S(L) is increased by mutations at A3 in cis or in RATlp and XRNlp in trans, and is kinetically faster than 5.8S(S) synthesis.

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Section: Analysis Of the Effects Of Large Deletions In Its1mentioning

confidence: 95%

The 5′ end of yeast 5.8S rRNA is generated by exonucleases from an upstream cleavage site.

et al. 1994

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“…lc). One form, "5.8S A" rRNA, has 6 or 7 additional bases (3); the other, "5.8S B" rRNA, has 149 additional bases (3,21 the primer region for mitochondrial DNA replication (25,26). However, only a minute fraction of the NME1/7-2 RNA is located in the mitochondria (27,28).…”

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confidence: 99%

“…Strains and Plasmids. Strains YLL53 (MATa,his3A200,tyri,RRP2) and YLL54 [MATa,his3A200,lys2, were derived from sibling spores of a single tetrad obtained in the second backcross of the rrp2-2 mutant to its parent (3). Strain KS7-1D [MATa,ade2,ura3,leu2, trpl, rrp2-1 (temperature-sensitive)] (21) was kindly provided by Jon Warner (Albert Einstein College of Medicine).…”

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confidence: 99%

“…Strain KS7-1D [MATa,ade2,ura3,leu2, trpl, rrp2-1 (temperature-sensitive)] (21) was kindly provided by Jon Warner (Albert Einstein College of Medicine). The rrp2-1 and rrp2-2 mutants were isolated independently from different collections of temperature-sensitive strains but were shown to be allelic by virtue of their identical rRNA processing phenotypes and failure to complement each other (3,21). The YCplac33 cloning vector contains the CEN4, ARSI, and URA3 sequences of S. cerevisiae (32) and was obtained from C. H. Sommers and S. Prakash (University of Rochester).…”

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confidence: 99%

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The RNA of RNase MRP is required for normal processing of ribosomal RNA.

Chu

Archer

Zengel

et al. 1994

Proc. Natl. Acad. Sci. U.S.A.

211

161

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We have isolated clones which complement the temperature sensitivity and abnormal rRNA processing pattern of the rrp2-2 mutant of Saccharomyces cerevisiae we previously described. DNA sequencing and restriction analysis demonstrated that all clones contain the NMEI gene encoding the RNA of the ribonucleoprotein particle RNase MRP. Deletion analysis showed that the NMEI gene is responsible for the complementation of the rrp2-2 phenotype. A single base change was identified in the nmel gene in the rrp2 mutant, confirming that the RRP2 and NMEI genes are identical. Our experiments therefore indicate that RNase MRP, in addition to its previously reported role in formation of RNA primers for mitochondrial DNA replication [Clayton, D. A. (1991) Trends Biochem. Sci. 16, 107-111], is involved in rRNA processing.

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“…Heat-and cold-sensitive mutants that have ribosomal subunit deficits have been identified by monitoring changes in the steady-state levels of ribosomal subunits, although in most cases the corresponding genes have not been cloned (3,7,17,54,56). Two temperature-sensitive mutants of S. cerevisiae that fail to process rRNA have been isolated, although steady-state levels of ribosomal subunits have not been examined (30,52).…”

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DRS1 to DRS7, novel genes required for ribosome assembly and function in Saccharomyces cerevisiae.

Ripmaster¹,

Vaughn²,

Woolford³

1993

Mol. Cell. Biol.

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To identify Saccharomyces cerevisiae mutants defective in assembly or function of ribosomes, a collection of cold-sensitive strains generated by treatment with ethyl methanesulfonate was screened by sucrose gradient analysis for altered ratios of free 40S to 60S ribosomal subunits or qualitative changes in polyribosome profiles. Mutations The eukaryotic ribosome is a complex organelle which in most species contains more than 75 different proteins and four different RNA molecules. The primary sequences of eukaryotic rRNAs and many eukaryotic ribosomal proteins (r-proteins) (reviewed in references 65 and 66) have been determined or inferred from sequences of the respective genes. Regulation of expression of these genes has been studied in some detail (65,66). Despite the large volume of data concerning the structure and expression of individual components of eukaryotic ribosomes, the pathway of assembly of ribosomal subunits and the functional roles that r-proteins and rRNAs play during the translation process are not well understood.Ribosome biogenesis occurs in the nucleolus of eukaryotic cells, where rRNA is transcribed and processed, and associates with r-proteins imported from the cytoplasm (reviewed in references 19, 65, and 66). Preribosomal particles containing rRNA precursors, r-proteins, and non-r-proteins have been detected within the nucleolus (59, 63). Most of the r-proteins assemble into subunits while in the nucleolus, although some final steps of maturation occur after transport of subunits to the cytoplasm (61). The ribosomal subunits are then competent to catalyze protein synthesis.Reconstitution and genetic studies have been applied successfully to study the ribosome assembly pathway in prokaryotic cells. Functional 30S and 50S ribosomal subunits of Escherichia coli can be reconstituted from purified rRNA and r-proteins in vitro (38,60

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A new rRNA processing mutant ofSaccharomyces cerevisiae

Cited by 70 publications

References 31 publications

The 5′ end of yeast 5.8S rRNA is generated by exonucleases from an upstream cleavage site.

The 5′ end of yeast 5.8S rRNA is generated by exonucleases from an upstream cleavage site.

The RNA of RNase MRP is required for normal processing of ribosomal RNA.

DRS1 to DRS7, novel genes required for ribosome assembly and function in Saccharomyces cerevisiae.

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