The <i>Saccharomyces cerevisiae</i> RNase Mitochondrial RNA Processing Is Critical for Cell Cycle Progression at the End of Mitosis

Cai, Ti; Aulds, Jason; Gill, Tina; Cerio, Michael; Schmitt, Michael N.

doi:10.1093/genetics/161.3.1029

Cited by 67 publications

(5 citation statements)

References 45 publications

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“…This discrepancy has led to the suggestion that RNase MRP has other functions in the cell. In particular, a correlation between RNase MRP activity and cell division has been reported previously (8)(9)(10). We therefore compared the morphology of cells carrying the Mini2 mutation, or Mini2 and the pop4-8 suppressor, with wild-type cells after a shift to 37 C. After 4 h, there was essentially no effect.…”

Section: Suppression Of the Mini2 Defectmentioning

confidence: 78%

“…A typical phenotype of RNase MRP mutants is an increased 5.8S L to 5.8S S ratio and aberrant accumulation of a very long 5.8S rRNA, which is 149 nt longer at the 5 0 end than the 5.8S S rRNA (1,4) and corresponds to the product of cleavage at a site (A2) upstream of the RNase MRP cleavage site A3. RNase MRP has also been implicated in primer formation for mitochondrial DNA replication (7) and cell cycle control (8)(9)(10).…”

Section: Introductionmentioning

confidence: 99%

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Identification of a functional core in the RNA component of RNase MRP of budding yeasts

2004

Nucleic Acids Research

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RNase MRP is an endonuclease participating in ribosomal RNA processing. It consists of one RNA and at least nine protein subunits. Using oligonucleotide-directed mutagenesis, we analyzed the functional role of five of the hairpins in the secondary structure of the RNA subunit of Saccharomyces cerevisiae RNase MRP. Deletion of an entire hairpin was either lethal or resulted in very poor growth. However, peripheral portions constituting up to 70% of a hairpin could be deleted without effects on cell growth rate or processing of rRNA. To determine whether these hairpins perform redundant functions, we analyzed mutants combining four or five benign hairpin deletions. Simultaneous removal of four of these hairpin segments had no detectable effect. Removing five created a temperature- and cold-sensitive enzyme, but these deficiencies could be partially overcome by a mutation in one of the RNase MRP protein subunits, or by increasing the copy number of several of the protein subunit genes. These observations suggest that the peripheral elements of the RNA hairpins contain no structures or sequences required for substrate recognition, catalysis or binding of protein subunits. Thus, the functionally essential elements of the RNase MRP RNA appear to be concentrated in the core of the subunit.

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Section: Suppression Of the Mini2 Defectmentioning

confidence: 78%

Section: Introductionmentioning

confidence: 99%

Identification of a functional core in the RNA component of RNase MRP of budding yeasts

2004

Nucleic Acids Research

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“…RNase P is closely related to another ribonucleoprotein complex, RNase MRP, which processes preribosomal RNA as part of the pathway toward appropriately posttranscriptionally modified ribosomal RNA in eukaryotes and also plays an essential role in yeast cell cycle progression ( − ). The RNA components of RNase MRP and RNase P are similar in terms of their primary and secondary structure, and each RNase contains some of the same protein components ( , ), although there is at least one protein component that is specific to each ( , ).…”

mentioning

confidence: 99%

NMR Structure of an Archaeal Homologue of Ribonuclease P Protein Rpp29

Sidote

Hoffman

2003

Biochemistry

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A protein component of the Archaeoglobus fulgidus RNase P was expressed in Escherichia coli, purified, and structurally characterized using multidimensional NMR methods. The dominant structural feature of this 11 kDa protein is a sheet of six antiparallel beta-strands, wrapped around a core of conserved hydrophobic amino acids. Amide proton exchange and (15)N relaxation rate data provide evidence that the first 16 residues of the protein, located before the start of the first beta-strand, and the last 24 residues, located past the end of the last beta-strand, are relatively flexible; this contrasts with the relatively rigid and well-defined structure of the beta-sheet. Amino acid sequence comparisons among a diverse set of species indicate that the A. fulgidus protein is homologous to the human RNase P protein Rpp29, yeast RNase P protein Pop4, and a known archaeal RNase P protein from Methanobacter thermoautotrophicus; conserved hydrophobic residues indicate that the homologous protein in each of these species contains a similar beta-sheet structure. Conserved surface residues located in the loop connecting strands beta2 and beta3, the loop connecting strands beta4 and beta5, and in the flexible N- and C-terminal tails are most likely to have specific interactions with the RNA and other proteins of RNase P. The structural model of an RNase P protein component provided by the present work provides an essential step toward eventually understanding the overall architecture of this complex enzyme and the mechanism by which it performs its functions.

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“…The transcription of one of those mitotic cyclins, CLB2, is controlled and increases as cells become closer to mitosis. Subsequently, entry into mitosis promotes rapid CLB2 mRNA decay that, if prevented, would avoid exit from mitosis [149,150]. The half-life of CLB2 drops more than 30-fold before metaphase.…”

Section: Torc1 Regulates Mitosis Progressionmentioning

confidence: 99%

TOR Complex 1: Orchestrating Nutrient Signaling and Cell Cycle Progression

Foltman,

Sanchez-Diaz

2023

IJMS

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The highly conserved TOR signaling pathway is crucial for coordinating cellular growth with the cell cycle machinery in eukaryotes. One of the two TOR complexes in budding yeast, TORC1, integrates environmental cues and promotes cell growth. While cells grow, they need to copy their chromosomes, segregate them in mitosis, divide all their components during cytokinesis, and finally physically separate mother and daughter cells to start a new cell cycle apart from each other. To maintain cell size homeostasis and chromosome stability, it is crucial that mechanisms that control growth are connected and coordinated with the cell cycle. Successive periods of high and low TORC1 activity would participate in the adequate cell cycle progression. Here, we review the known molecular mechanisms through which TORC1 regulates the cell cycle in the budding yeast Saccharomyces cerevisiae that have been extensively used as a model organism to understand the role of its mammalian ortholog, mTORC1.

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The Saccharomyces cerevisiae RNase Mitochondrial RNA Processing Is Critical for Cell Cycle Progression at the End of Mitosis

Cited by 67 publications

References 45 publications

Identification of a functional core in the RNA component of RNase MRP of budding yeasts

Identification of a functional core in the RNA component of RNase MRP of budding yeasts

NMR Structure of an Archaeal Homologue of Ribonuclease P Protein Rpp29

TOR Complex 1: Orchestrating Nutrient Signaling and Cell Cycle Progression

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