title: The 3' ends of mature transcripts are generated by a processosome complex in fission yeast mitochondria.
abstract: In this article, we report on the genetic analysis of the Schizosaccharomyces pombe open reading frames SPCC1322.01 and SPAC637.11, respectively, which encode proteins that are similar to the exoribonuclease Dss1p and the RNA helicase Suv3p, respectively, forming the mitochondrial degradosome of Saccharomyces cerevisiae. While the helicase Suv3p is exchangeable between S. cerevisiae and S. pombe, the functions of Dss1p and the putative fission yeast RNase protein are specific for each species. Unlike S. cerevisiae mutants lacking a functional degradosome, the major defect of fission yeast knock-out strains is their inability to perform downstream processing of transcripts. In addition, the lack of pah1 results in instability of mitochondrial RNA ends. Overexpression of par1 and pah1 has no significant effect on the steady-state levels of mitochondrial RNAs. The Pet127p-stimulated RNA degradation activity is independent of Par1p/Pah1p in fission yeast mitochondria. The results presented herein indicate that both fission yeast proteins play only a minor role (if at all) in mitochondrial RNA degradation. We assume that the RNA-degrading function was taken over by other enzymes in fission yeast mitochondria, while the former degradosome proteins were recruited to new cellular pathways, for example, RNA processing in fission yeast (as discussed in this article) or mitochondrial DNA replication, apoptosis, or chromatin maintenance in eukaryotes, during evolution.
authors.affiliation: Department of Biology IV (Microbiology and Genetics), RWTH Aachen University, Worringer Weg, D-52056 Aachen, Germany.
authors.forename: Bastian
authors.initials: B
authors.lastname: Hoffmann
authors.forename: Jens
authors.initials: J
authors.lastname: Nickel
authors.forename: Falk
authors.initials: F
authors.lastname: Speer
authors.forename: Bernd
authors.initials: B
authors.lastname: Schafer
mesh_terms: D002244:Carbon / Q000378:metabolism / Q000600:supply & distribution; D053487:DEAD-box RNA Helicases / Q000235:genetics / Q000502:physiology; D005095:Exoribonucleases; D005285:Fermentation / Q000502:physiology; D005656:Fungal Proteins / Q000235:genetics / Q000502:physiology; D015966:Gene Expression Regulation, Fungal; D015723:Gene Library; D005816:Genetic Complementation Test; D008928:Mitochondria / Q000235:genetics* / Q000378:metabolism; D046912:Multiprotein Complexes / Q000378:metabolism / Q000502:physiology; D016366:Open Reading Frames / Q000235:genetics / Q000502:physiology; D030781:Organisms, Genetically Modified; D010711:Phosphatidate Phosphatase / Q000235:genetics / Q000502:physiology; D010749:Phosphoprotein Phosphatases; D026721:RNA 3' End Processing / Q000502:physiology*; D012331:RNA, Fungal / Q000378:metabolism; D029701:Saccharomyces cerevisiae Proteins / Q000235:genetics / Q000502:physiology; D012568:Schizosaccharomyces / Q000235:genetics* / Q000254:growth & development / Q000378:metabolism; D029702:Schizosaccharomyces pombe Proteins / Q000235:genetics / Q000502:physiology; D015854:Up-Regulation; D039221:mRNA Cleavage and Polyadenylation Factors / Q000378:metabolism / Q000502:physiology*
chemical_list: D005656:Fungal Proteins; D046912:Multiprotein Complexes; C410165:PAR1 protein, S pombe; D012331:RNA, Fungal; D029701:Saccharomyces cerevisiae Proteins; D029702:Schizosaccharomyces pombe Proteins; D039221:mRNA Cleavage and Polyadenylation Factors; D002244:Carbon; D005095:Exoribonucleases; C098317:DSS1 protein, S cerevisiae; D010749:Phosphoprotein Phosphatases; D010711:Phosphatidate Phosphatase; C075918:SUV3 protein, S cerevisiae; D053487:DEAD-box RNA Helicases