Requirement of Fission Yeast Cid14 in Polyadenylation of rRNAs

Win, Thein Z.; Draper, Simon J.; Read, Rebecca L.; Pearce, J. W.; Norbury, Chris J.; Wang, Shao-Win

doi:10.1128/mcb.26.5.1710-1721.2006

Cited by 75 publications

(106 citation statements)

References 54 publications

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“…In vivo it is part of the TRAMP4 complex that contains Trf4p as the catalytic subunit, one of the zinc knuckle proteins Air1p or Air2p, thought to confer the RNA-binding function to the complex, and the RNA helicase Mtr4p (LaCava et al 2005;Vanacova et al 2005). A similar complex, SpTRAMP, was identified in fission yeast (Win et al 2006;Bühler et al 2008). In Drosophila melanogaster, overexpression of a homolog of Trf4p was shown to lead to the polyadenylation of snRNAs (Nakamura et al 2008), whereas the human homolog PAPD5 is involved in the polyadenylation-mediated degradation of aberrant prerRNAs (Shcherbik et al 2010).…”

Section: Introductionmentioning

confidence: 99%

PAPD5, a noncanonical poly(A) polymerase with an unusual RNA-binding motif

Rammelt¹,

Bilen²,

Zavolan³

et al. 2011

RNA

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PAPD5 is one of the seven members of the family of noncanonical poly(A) polymerases in human cells. PAPD5 was shown to polyadenylate aberrant pre-ribosomal RNAs in vivo, similar to degradation-mediating polyadenylation by the noncanonical poly(A) polymerase Trf4p in yeast. PAPD5 has been reported to be also involved in the uridylation-dependent degradation of histone mRNAs. To test whether PAPD5 indeed catalyzes adenylation as well as uridylation of RNA substrates, we analyzed the in vitro properties of recombinant PAPD5 expressed in mammalian cells as well as in bacteria. Our results show that PAPD5 catalyzes the polyadenylation of different types of RNA substrates in vitro. Interestingly, PAPD5 is active without a protein cofactor, whereas its yeast homolog Trf4p is the catalytic subunit of a bipartite poly(A) polymerase in which a separate RNAbinding subunit is needed for activity. In contrast to the yeast protein, the C terminus of PAPD5 contains a stretch of basic amino acids that is involved in binding the RNA substrate.

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Section: Introductionmentioning

confidence: 99%

PAPD5, a noncanonical poly(A) polymerase with an unusual RNA-binding motif

Rammelt¹,

Bilen²,

Zavolan³

et al. 2011

RNA

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“…To test whether the poly(A) polymerase activity of TRAMP was required for Pab2-dependent regulation of meiRNA, we deleted cid14, which encodes the single catalytic subunit of the fission yeast TRAMP complex (42,43). Deletion of cid14 did not result in detectable levels of meiRNA (Fig.…”

Section: Meiotic Differentiationmentioning

confidence: 99%

Negative Regulation of Meiotic Gene Expression by the Nuclear Poly(a)-binding Protein in Fission Yeast

St-André

Lemieux

Perreault

et al. 2010

Journal of Biological Chemistry

105

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Meiosis is a cellular differentiation process in which hundreds of genes are temporally induced. Because the expression of meiotic genes during mitosis is detrimental to proliferation, meiotic genes must be negatively regulated in the mitotic cell cycle. Yet, little is known about mechanisms used by mitotic cells to repress meiosis-specific genes. Here we show that the poly(A)-binding protein Pab2, the fission yeast homolog of mammalian PABPN1, controls the expression of several meiotic transcripts during mitotic division. Our results from chromatin immunoprecipitation and promoter-swapping experiments indicate that Pab2 controls meiotic genes post-transcriptionally. Consistently, we show that the nuclear exosome complex cooperates with Pab2 in the negative regulation of meiotic genes. We also found that Pab2 plays a role in the RNA decay pathway orchestrated by Mmi1, a previously described factor that functions in the post-transcriptional elimination of meiotic transcripts. Our results support a model in which Mmi1 selectively targets meiotic transcripts for degradation via Pab2 and the exosome. Our findings have therefore uncovered a mode of gene regulation whereby a poly(A)-binding protein promotes RNA degradation in the nucleus to prevent untimely expression.Meiosis is a key differentiation process essential for the generation of genetically distinct individuals. During yeast meiosis, two cells of opposite mating types fuse and conjugate their DNA to form a diploid cell. This diploid cell undergoes DNA replication followed by two rounds of cell division to produce four haploid cells. Although many of the activities used to achieve cell division are common to both meiosis and mitosis, there are several features unique to meiosis. Importantly, the meiotic and mitotic cell cycles are mutually exclusive, and genes required for meiotic differentiation are solely expressed during meiosis. Such negative control of meiotic genes during mitosis suggests important regulatory systems to avoid inappropriate activation of meiosis. To date, however, the molecular mechanisms by which meiotic differentiation genes are suppressed during the mitotic cell cycle remain poorly understood.In the fission yeast Schizosaccharomyces pombe, meiotic differentiation involves the temporal activation of hundreds of genes (1). Although previous studies have established the importance of transcriptional regulation during fission yeast meiosis (1, 2), recent results implicate post-transcriptional mechanisms of gene regulation, including pre-mRNA splicing and mRNA degradation. Accordingly, several meiotic genes are specifically spliced during meiosis, but remain unspliced during the mitotic cell cycle (3, 4). Selective mRNA turnover is another mechanism used by fission yeast to ensure the absence of meiosis-specific transcripts during the mitotic cell cycle. The rapid elimination of specific meiotic transcripts in mitotic cells requires the YTH-family RNA-binding protein, Mmi1 (5). Mmi1 promotes the destruction of specific meiotic transcripts...

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“…Homologs of Trf4 and Trf5 exist in eukaryotes from yeast to humans, though only the Cid14 from Schizosaccharomyces pombe, which forms a similar TRAMP complex with homologs to Air1 and Mtr4, has been shown to be functionally homologous to the Trf proteins from S. cerevisiae (Aravind and Koonin 1999;Saitoh et al 2002;Win et al 2006;Buhler et al 2007;Wang et al 2008). Humans contain two Trf homologs, PAPD5 and PAPD7, both of which exhibit 37% identity to the catalytic domain of S. cerevisiae Trf4.…”

Section: Introductionmentioning

confidence: 99%

Air proteins control differential TRAMP substrate specificity for nuclear RNA surveillance

Schmidt

Mathews

et al. 2012

RNA

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RNA surveillance systems function at critical steps during the formation and function of RNA molecules in all organisms. The RNA exosome plays a central role in RNA surveillance by processing and degrading RNA molecules in the nucleus and cytoplasm of eukaryotic cells. The exosome functions as a complex of proteins composed of a nine-member core and two ribonucleases. The identity of the molecular determinants of exosome RNA substrate specificity remains an important unsolved aspect of RNA surveillance. In the nucleus of Saccharomyces cerevisiae, TRAMP complexes recognize and polyadenylate RNAs, which enhances RNA degradation by the exosome and may contribute to its specificity. TRAMPs contain either of two putative RNA-binding factors called Air proteins. Previous studies suggested that these proteins function interchangeably in targeting the poly(A)-polymerase activity of TRAMPs to RNAs. Experiments reported here show that the Air proteins govern separable functions. Phenotypic analysis and RNA deep-sequencing results from air mutants reveal specific requirements for each Air protein in the regulation of the levels of noncoding and coding RNAs. Loss of these regulatory functions results in specific metabolic and plasmid inheritance defects. These findings reveal differential functions for Air proteins in RNA metabolism and indicate that they control the substrate specificity of the RNA exosome.

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Requirement of Fission Yeast Cid14 in Polyadenylation of rRNAs

Cited by 75 publications

References 54 publications

PAPD5, a noncanonical poly(A) polymerase with an unusual RNA-binding motif

PAPD5, a noncanonical poly(A) polymerase with an unusual RNA-binding motif

Negative Regulation of Meiotic Gene Expression by the Nuclear Poly(a)-binding Protein in Fission Yeast

Air proteins control differential TRAMP substrate specificity for nuclear RNA surveillance

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