Assembly into snoRNP controls 5′-end maturation of a box C/D snoRNA in Saccharomyces cerevisiae

Preti, Milena; Guffanti, Elisa; Valitutto, Eleonora; Dieci, Giorgio

doi:10.1016/j.bbrc.2006.10.053

Cited by 8 publications

(6 citation statements)

References 26 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The lower levels of pre-and mature RPR1 and SNR52 RNAs detected in the KE mutant in vivo likely stem from a combination of their non-canonical type 2 promoter structure, their unique processing and/or a requirement for specific RNA binding proteins to prevent their degradation (Lygerou et al, 1994;Srisawat et al, 2002;Preti et al, 2006;Palsule et al, 2019).…”

Section: Discussionmentioning

confidence: 99%

“…Both RPR1 and SNR52 are synthesized as precursor RNAs from tRNA-like promoter elements that are positioned upstream of the mature RNAs and thus produce precursor RNAs with long 5' leader sequences (Lee et al, 1991b;Harismendy et al, 2003;Lee et al, 2003;Preti et al, 2006). Although both genes contain A-and B-box internal promoter elements, the B-box in RPR1 deviates from consensus (Lee et al, 1991a) and the distance between the boxes in SNR52 is significantly longer than is typical.…”

Section: Discussionmentioning

confidence: 99%

See 1 more Smart Citation

Functional characterization of Polr3a hypomyelinating leukodystrophy mutations in the S. cerevisiae homolog, RPC160

Moir

Lavados

Lee

et al. 2021

Gene

View full text Add to dashboard Cite

Mutations in RNA polymerase III (Pol III) cause hypomeylinating leukodystrophy (HLD) and neurodegeneration in humans. POLR3A and POLR3B, the two largest Pol III subunits, together form the catalytic center and carry the majority of disease alleles. Disease-causing mutations include invariant and highly conserved residues that are predicted to negatively affect Pol III activity and decrease transcriptional output. A subset of HLD missense mutations in POLR3A cluster in the pore region that provides nucleotide access to the Pol III active site. These mutations were engineered at the corresponding positions in the Saccharomyces cerevisiae homolog, Rpc160, to evaluate their functional deficits. None of the mutations caused a growth or transcription phenotype in yeast. Each mutation was combined with a frequently occurring pore mutation, POLR3A G672E, which was also wild-type for growth and transcription. The double mutants showed a spectrum of phenotypes from wild-type to lethal, with only the least fit combinations showing an effect on Pol III transcription. In one slow-growing temperaturesensitive mutant the steady-state level of tRNAs was unaffected, however global tRNA synthesis was compromised, as was the synthesis of RPR1 and SNR52 RNAs. Affinity-purified mutant Pol III was broadly defective in both factor-independent and factor-dependent transcription in vitro across genes that represent the yeast Pol III transcriptome. Thus, the robustness of yeast to Pol III leukodystrophy mutations in RPC160 can be overcome by a combinatorial strategy..

show abstract

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Functional characterization of Polr3a hypomyelinating leukodystrophy mutations in the S. cerevisiae homolog, RPC160

Moir

Lavados

Lee

et al. 2021

Gene

View full text Add to dashboard Cite

show abstract

“…Detailed re-analysis of the C. elegans tiling microarray data [ 34 ] indicated the existence of similar primary transcripts arising from several genomic UM2 loci, and subsequent 3'RACE verified this. The fact that a UM2-containing primary transcript could not be identified at all inspected loci (including the endogenous CeN37 locus used for the reporter construct) could owe to the primary transcripts being inherently unstable and rapidly degraded during snoRNA maturation [ 33 ]. The C. elegans UM2 primary transcripts resemble the dicstronic tRNA-snoRNA transcripts found at a few plant and yeast loci [ 29 , 32 , 55 , 56 ].…”

Section: Discussionmentioning

confidence: 99%

“…It is possible that UM2 is derived from tRNA genes that have served as promoters for downstream ncRNA genes, as similar tRNA-snoRNA dicistronic transcriptional structures have been described in plants and yeast [ 29 - 32 ]. Most of the UM2 loci encode snoRNAs which generally produce uncapped transcripts terminated at an oligo-T tract, and are thus likely to be transcribed by polymerase III [ 6 ], though the lack of a cap could also be due to processing of the primary snoRNA transcript [ 32 , 33 ].…”

Section: Introductionmentioning

confidence: 99%

In vivo analysis of Caenorhabditis elegans noncoding RNA promoter motifs

Wang

et al. 2008

BMC Mol Biol

View full text Add to dashboard Cite

show abstract

“…Nop1p has also been shown to influence Rnt1p cleavage of pre-U18 snoRNA (32). The assembly of snoRNP has also been shown to be coupled to 5Ј-end maturation of independently transcribed box C/D snoRNAs (60).…”

Section: Discussionmentioning

confidence: 99%

Cwc24p, a Novel Saccharomyces cerevisiae Nuclear Ring Finger Protein, Affects Pre-snoRNA U3 Splicing

Goldfeder¹,

Oliveira

2008

Journal of Biological Chemistry

View full text Add to dashboard Cite

U3 snoRNA is transcribed from two intron-containing genes in yeast, snR17A and snR17B. Although the assembly of the U3 snoRNP has not been precisely determined, at least some of the core box C/D proteins are known to bind pre-U3 co-transcriptionally, thereby affecting splicing and 3-end processing of this snoRNA. We identified the interaction between the box C/D assembly factor Nop17p and Cwc24p, a novel yeast RING finger protein that had been previously isolated in a complex with the splicing factor Cef1p. Here we show that, consistent with the protein interaction data, Cwc24p localizes to the cell nucleus, and its depletion leads to the accumulation of both U3 pre-snoRNAs. U3 snoRNA is involved in the early cleavages of 35 S pre-rRNA, and the defective splicing of pre-U3 detected in cells depleted of Cwc24p causes the accumulation of the 35 S precursor rRNA. These results led us to the conclusion that Cwc24p is involved in pre-U3 snoRNA splicing, indirectly affecting pre-rRNA processing.In eukaryotes, three of the rRNAs (18, 5.8, and 25 S in the yeast Saccharomyces cerevisiae) are transcribed by RNA pol 3 I as a single precursor, which undergoes various processing steps that include nucleotide modifications and endo-and exonucleolytic cleavages. In yeast, at least 150 factors are involved in 35 S pre-rRNA processing, including different proteins and snoRNPs. Processing and modification of the pre-rRNA seems to occur simultaneously with the assembly of ribosomal proteins, and large transient ribonucleoprotein (RNP) particles are formed in the nucleolus (1-3). Different sets of proteins were found in each complex. Among the proteins identified in the 90 S preribosomal complex are many of the small subunit ribosomal proteins, the core box C/D proteins (Nop1p, Nop56p, and Nop58p), U3 snoRNP-specific proteins, and other factors that might also be involved in the early steps of pre-rRNA processing (2). Proteins present in the pre-60 S complex are mainly involved in processing of 5.8 S and 25 S and in the formation of the large ribosome subunit (4, 5).

show abstract

Assembly into snoRNP controls 5′-end maturation of a box C/D snoRNA in Saccharomyces cerevisiae

Cited by 8 publications

References 26 publications

Functional characterization of Polr3a hypomyelinating leukodystrophy mutations in the S. cerevisiae homolog, RPC160

Functional characterization of Polr3a hypomyelinating leukodystrophy mutations in the S. cerevisiae homolog, RPC160

In vivo analysis of Caenorhabditis elegans noncoding RNA promoter motifs

Cwc24p, a Novel Saccharomyces cerevisiae Nuclear Ring Finger Protein, Affects Pre-snoRNA U3 Splicing

Contact Info

Product

Resources

About