RNAPub Date : 2025-02-07DOI: 10.1261/rna.080350.124
Michał Brouze, Marcin Szpila, Areta Magdalena Czerwińska, Wiktor Antczak, Seweryn Mroczek, Tomasz Kuliński, Anna Maria Hojka-Osińska, Dominik Cysewski, Olga Gewartowska, Dorota Adamska, Jakub Gruchota, Ewa Borsuk, Andrzej Dziembowski
{"title":"DIS3L, cytoplasmic exosome catalytic subunit, is essential for development but not cell viability in mice.","authors":"Michał Brouze, Marcin Szpila, Areta Magdalena Czerwińska, Wiktor Antczak, Seweryn Mroczek, Tomasz Kuliński, Anna Maria Hojka-Osińska, Dominik Cysewski, Olga Gewartowska, Dorota Adamska, Jakub Gruchota, Ewa Borsuk, Andrzej Dziembowski","doi":"10.1261/rna.080350.124","DOIUrl":"https://doi.org/10.1261/rna.080350.124","url":null,"abstract":"<p><p>Among numerous enzymes involved in RNA decay, processive exoribonucleases are the most prominent group responsible for the degradation of the entire RNA molecules. The role of mammalian cytoplasmic 3'-5' exonuclease DIS3L at the organismal level remained unknown. Herein, we established knock-in and knock-out mouse models to study DIS3L functions in mice. DIS3L in mice is indeed a subunit of the cytoplasmic exosome complex, the disruption of which leads to severe embryo degeneration and death in mice soon after implantation. These changes could not be prevented by supplementing extraembryonic tissue with functional DIS3L through the construction of chimeric embryos. Preimplantation Dis3l-/- embryos were unaffected in their morphology and ability to produce functional embryonic stem cells, showing that DIS3L is not essential for cell viability. There were also no major changes at the transcriptome level for both embryonic stem cells and blastocysts, as revealed by RNA sequencing experiments. Notably, however, Dis3l knock-out led to inhibition of the global protein synthesis. These results point to the essential role of DIS3L in mRNA metabolism, which is crucial for proper protein synthesis during embryo development.</p>","PeriodicalId":21401,"journal":{"name":"RNA","volume":" ","pages":""},"PeriodicalIF":4.2,"publicationDate":"2025-02-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143371194","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
RNAPub Date : 2025-02-07DOI: 10.1261/rna.080406.125
Susan Gerbi
{"title":"Retrospective Article: Joseph G. Gall (1928-2024).","authors":"Susan Gerbi","doi":"10.1261/rna.080406.125","DOIUrl":"https://doi.org/10.1261/rna.080406.125","url":null,"abstract":"","PeriodicalId":21401,"journal":{"name":"RNA","volume":" ","pages":""},"PeriodicalIF":4.2,"publicationDate":"2025-02-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143370284","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
RNAPub Date : 2025-01-29DOI: 10.1261/rna.080272.124
Hanna Alalam, Monika Safhauzer, Per Sunnerhagen
{"title":"New reporters for monitoring cellular NMD.","authors":"Hanna Alalam, Monika Safhauzer, Per Sunnerhagen","doi":"10.1261/rna.080272.124","DOIUrl":"https://doi.org/10.1261/rna.080272.124","url":null,"abstract":"<p><p>Nonsense-mediated decay (NMD) is a eukaryotic surveillance pathway that controls degradation of cytoplasmic transcripts with aberrant features. NMD-controlled RNA degradation acts to regulate a large fraction of the mRNA population. It has been implicated in cellular responses to infections and environmental stress, as well as in deregulation of tumor-promoting genes. NMD is executed by a set of three core factors conserved in evolution, UPF1-3, as well as additional influencing proteins such as kinases. Monitoring NMD activity is challenging due to the difficulties in quantitating RNA decay rates in vivo, and consequently it has also been problematic to identify new factors influencing NMD. Here, we developed a genetic selection system in yeast to capture new components affecting NMD status. The reporter constructs link NMD target sequences with nutrient-selectable genetic markers. By crossing these reporters into a genome-wide library of deletion mutants and quantitating colony growth on selective medium, we robustly detect previously known NMD components in a high-throughput fashion. In addition, we identify novel mutations influencing NMD status and implicate ribosome recycling as important for NMD. By using our constructed combinations of promoters, NMD target sequences, and selectable markers, the system can also efficiently detect mutations with a minor effect, or in special environments. Furthermore, it can be used to explore how NMD acts on targets of different structures.</p>","PeriodicalId":21401,"journal":{"name":"RNA","volume":" ","pages":""},"PeriodicalIF":4.2,"publicationDate":"2025-01-29","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143067906","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
RNAPub Date : 2025-01-28DOI: 10.1261/rna.080335.124
Sepideh Fakhretaha Aval, Amal Seffouh, Kyung-Mee Moon, Leonard Foster, Joaquin Ortega, Kurt Fredrick
{"title":"Role of the sarcin-ricin loop of 23S rRNA in biogenesis of the 50S ribosomal subunit.","authors":"Sepideh Fakhretaha Aval, Amal Seffouh, Kyung-Mee Moon, Leonard Foster, Joaquin Ortega, Kurt Fredrick","doi":"10.1261/rna.080335.124","DOIUrl":"https://doi.org/10.1261/rna.080335.124","url":null,"abstract":"<p><p>The sarcin-ricin loop (SRL) is one of the most conserved segments of ribosomal RNA (rRNA). Translational GTPases (trGTPases), such as EF-G and EF-Tu and IF2, form contacts with the SRL that are critical for GTP hydrolysis and factor function. Previous studies showed that expression of 23S rRNA lacking the SRL confers a dominant lethal phenotype in E. coli. Isolated ΔSRL particles were found to be not only inactive in protein synthesis but also incompletely assembled. In particular, block 4 of the subunit, which includes the peptidyl transferase center, remained unfolded. Here, we explore the basis of this assembly defect. We find that 23S rRNA extracted from ΔSRL subunits can be efficiently reconstituted into 50S subunits, and these reconstituted ΔSRL particles exhibit full peptidyl transferase activity. We also further characterize ΔSRL particles purified from cells, using cryo-EM and proteomic methods. These particles lack density for rRNA and r-proteins of block 4, consistent with earlier chemical probing data. Incubation of these particles with excess total r-protein of the large subunit (TP50) fails to restore substantial peptidyl transferase activity. Interestingly, proteomic analysis of control and mutant particles shows an overrepresentation of multiple assembly factors in the ΔSRL case. We propose that one or more GTPases normally act to release assembly factors, and this activity is blocked in the absence of the SRL.</p>","PeriodicalId":21401,"journal":{"name":"RNA","volume":" ","pages":""},"PeriodicalIF":4.2,"publicationDate":"2025-01-28","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143060505","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
RNAPub Date : 2025-01-28DOI: 10.1261/rna.080207.124
Maciej M Basczok, Mikolaj Olejniczak
{"title":"RNA recognition by minimal ProQ from Neisseria meningitidis.","authors":"Maciej M Basczok, Mikolaj Olejniczak","doi":"10.1261/rna.080207.124","DOIUrl":"https://doi.org/10.1261/rna.080207.124","url":null,"abstract":"<p><p>Neisseria meningitidis minimal ProQ is a global RNA binding protein belonging to the family of FinO-domain proteins. The N. meningitidis ProQ consists only of the FinO domain accompanied by short N- and C-terminal extensions. To better understand how this minimal FinO-domain protein recognizes RNAs, we compared its binding to seven different natural RNA ligands of this protein. Next, two of these RNAs, rpmG-3' and AniS, were subject to further mutational studies. The data showed that N. meningitidis ProQ binds the lower part of the intrinsic transcription terminator hairpin, and that the single-stranded sequences on the 5' and 3' side of terminator stem are required for tight binding. However, the specific lengths of 5' and 3' RNA sequences required for optimal binding differed between the two RNAs. Additionally, our data show that the 2'-OH and 3'-OH groups of the 3' terminal ribose contribute to RNA binding by N. meningitidis ProQ. In summary, the minimal ProQ protein from N. meningitidis has generally similar requirements for RNA binding as the isolated FinO domains of other proteins of this family, but differs from them in detailed RNA features that are optimal for specific RNA recognition.</p>","PeriodicalId":21401,"journal":{"name":"RNA","volume":" ","pages":""},"PeriodicalIF":4.2,"publicationDate":"2025-01-28","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143060480","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
RNAPub Date : 2025-01-23DOI: 10.1261/rna.080315.124
Franziska Stegemann, Erin Marcus, Savanah Neupert, Sarah Ostrowski, David H Mathews, Eric M Phizicky
{"title":"Schizosaccharomyces pombe pus1 mutants are temperature sensitive due to decay of tRNAIle(UAU) by the 5'-3' exonuclease Dhp1, primarily targeting the unspliced pre-tRNA.","authors":"Franziska Stegemann, Erin Marcus, Savanah Neupert, Sarah Ostrowski, David H Mathews, Eric M Phizicky","doi":"10.1261/rna.080315.124","DOIUrl":"https://doi.org/10.1261/rna.080315.124","url":null,"abstract":"<p><p>The pseudouridylase Pus1 catalyzes pseudouridine (Ψ) formation at multiple uridine residues in tRNAs, and in some snRNAs and mRNAs. Although Pus1 is highly conserved, and mutations are associated with human disease, little is known about eukaryotic Pus1 biology. Here, we show that Schizosaccharomyces pombe pus1Δ mutants are temperature sensitive due to decay of tRNAIle(UAU), as tRNAIle(UAU) levels are reduced, and its overexpression suppresses the defect. We show that tRNAIle(UAU) is degraded by the 5'-3' exonuclease Dhp1 (ortholog of Saccharomyces cerevisiae Rat1), as each of four spontaneous pus1Δ suppressors had dhp1 mutations and restored tRNAIle(UAU) levels, and two suppressors that also restored tRNAIle(UAU) levels had mutations in tol1 (S. cerevisiae MET22 ortholog), predicted to inhibit Dhp1. We show that Pus1 modifies U27, U34, and U36 of tRNAIle(UAU), raising the question about how these modifications prevent decay. Our results suggests that Dhp1 targets unspliced pre-tRNAIle(UAU), as a pus1Δ strain in which the only copy of tRNAIle(UAU) has no intron (tI(UAU)-iΔ) is temperature resistant and undergoes no detectable decay, and the corresponding pus1Δ tI(UAU)-WT strain accumulates unspliced pre-tRNAIle(UAU). Moreover, the predicted exon-intron structure of pre-tRNAIle(UAU) differs from the canonical bulge-helix-loop structure compatible with tRNA splicing, and a pus1Δ tI(UAU)i-var strain with intron mutations predicted to improve exon-intron structure is temperature resistant and undergoes little decay. These results suggest that decay of tRNAIle(UAU) by Dhp1 in pus1Δ strains occurs at the level of unspliced pre-tRNAIle(UAU), implying a substantial role for one or more of the Ψ residues in stabilizing the pre-tRNA structure for splicing.</p>","PeriodicalId":21401,"journal":{"name":"RNA","volume":" ","pages":""},"PeriodicalIF":4.2,"publicationDate":"2025-01-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143029578","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
RNAPub Date : 2025-01-23DOI: 10.1261/rna.080290.124
Ugo Szachnowski, Emmanuelle Becker, Igor Stuparevic, Maxime Wery, Olivier Sallou, Mateo Boudet, Anthony Bretaudeau, Antonin Morillon, Michael Primig
{"title":"Pervasive formation of double-stranded RNAs by overlapping sense/antisense transcripts in budding yeast mitosis and meiosis.","authors":"Ugo Szachnowski, Emmanuelle Becker, Igor Stuparevic, Maxime Wery, Olivier Sallou, Mateo Boudet, Anthony Bretaudeau, Antonin Morillon, Michael Primig","doi":"10.1261/rna.080290.124","DOIUrl":"https://doi.org/10.1261/rna.080290.124","url":null,"abstract":"<p><p>Previous RNA profiling studies revealed co-expression of overlapping sense/antisense (s/a) transcripts in pro- and eukaryotic organisms. Functional analyses in yeast have shown that certain s/a mRNA/mRNA and mRNA/lncRNA pairs form stable double-stranded RNAs (dsRNAs) that affect transcript stability. Little is known, however, about the genome-wide prevalence of dsRNA formation and its potential functional implications during growth and development in diploid budding yeast. To address this question, we monitored dsRNAs in a Saccharomyces cerevisiae strain expressing the ribonuclease DCR1 and the RNA binding protein AGO1 from Naumovozyma castellii. We identify dsRNAs at 347 s/a loci that express partially or completely overlapping transcripts during mitosis, meiosis or both stages of the diploid life cycle. We associate dsRNAs with s/a loci previously thought to be exclusively regulated by antisense interference, and others that encode antisense RNAs, which downregulate sense mRNA-encoded protein levels. To facilitate hypothesis building we developed the Sense/Antisense double-stranded RNA (SensR) expression viewer. Users are able to retrieve different graphical displays of dsRNA and RNA expression data using genome coordinates and systematic or standard names for mRNAs and different types of stable or cryptic long non-coding RNAs (lncRNAs). Our data are a useful resource for improving yeast genome annotation and for work on RNA-based regulatory mechanisms controlling transcript and protein levels. The data are also interesting from an evolutionary perspective, since natural antisense transcripts that form stable dsRNAs have been detected in many species from bacteria to humans. The SensR viewer is freely accessible at https://sensr.genouest.org.</p>","PeriodicalId":21401,"journal":{"name":"RNA","volume":" ","pages":""},"PeriodicalIF":4.2,"publicationDate":"2025-01-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143029577","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
RNAPub Date : 2025-01-22DOI: 10.1261/rna.080310.124
Jiří Koubek, Jaswinder Kaur, Shivani Bhandarkar, Cole J T Lewis, Rachel O Niederer, Andrei Stanciu, Colin Echeverría Aitken, Wendy V Gilbert
{"title":"Cellular translational enhancer elements that recruit eukaryotic initiation factor 3.","authors":"Jiří Koubek, Jaswinder Kaur, Shivani Bhandarkar, Cole J T Lewis, Rachel O Niederer, Andrei Stanciu, Colin Echeverría Aitken, Wendy V Gilbert","doi":"10.1261/rna.080310.124","DOIUrl":"10.1261/rna.080310.124","url":null,"abstract":"<p><p>Translation initiation is a highly regulated process that broadly affects eukaryotic gene expression. Eukaryotic initiation factor 3 (eIF3) is a central player in canonical and alternative pathways for ribosome recruitment. Here, we have investigated how direct binding of eIF3 contributes to the large and regulated differences in protein output conferred by different 5'-untranslated regions (5' UTRs) of cellular mRNAs. Using an unbiased high-throughput approach to determine the affinity of budding yeast eIF3 for native 5' UTRs from 4252 genes, we demonstrate that eIF3 binds specifically to a subset of 5' UTRs that contain a short unstructured binding motif, AMAYAA. eIF3-binding mRNAs have higher ribosome density in growing cells and are preferentially translated under certain stress conditions, supporting the functional relevance of this interaction. Our results reveal a new class of translational enhancers and suggest a mechanism by which changes in core initiation factor activity enact mRNA-specific translation programs.</p>","PeriodicalId":21401,"journal":{"name":"RNA","volume":" ","pages":"193-207"},"PeriodicalIF":4.2,"publicationDate":"2025-01-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11789482/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142772143","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
RNAPub Date : 2025-01-22DOI: 10.1261/rna.080089.124
Tomasz Spiewla, Katarzyna Grab, Anais Depaix, Kamil Ziemkiewicz, Marcin Warminski, Jacek Jemielity, Joanna Kowalska
{"title":"An MST-based assay reveals new binding preferences of IFIT1 for canonically and noncanonically capped RNAs.","authors":"Tomasz Spiewla, Katarzyna Grab, Anais Depaix, Kamil Ziemkiewicz, Marcin Warminski, Jacek Jemielity, Joanna Kowalska","doi":"10.1261/rna.080089.124","DOIUrl":"10.1261/rna.080089.124","url":null,"abstract":"<p><p>IFITs (interferon-induced proteins with tetratricopeptide repeats) are components of the innate immune response that bind to viral and cellular RNA targets to inhibit translation and replication. The RNA target recognition is guided by molecular patterns, particularly at the RNA 5' ends. IFIT1 preferably binds RNAs modified with the m<sup>7</sup>G cap-0 structure, while RNAs with cap-1 structure are recognized with lower affinity. Less is known about the propensity of IFIT1 to recognize noncanonical RNA 5' ends, including hypermethylated and noncanonical RNA caps. Further insights into the structure-function relationship for IFIT1-RNA interactions are needed but require robust analytical methods. Here, we report a biophysical assay for quick, direct, in-solution affinity assessment of differently capped RNAs with IFIT1. The procedure, which relies on measuring microscale thermophoresis of fluorescently labeled protein as a function of increasing ligand concentration, is applicable to RNAs of various lengths and sequences without the need for their labeling or affinity tagging. Using the assay, we examined 13 canonically and noncanonically 5'-capped RNAs, revealing new binding preferences of IFIT1. The 5' terminal m<sup>6</sup>A mark in the m<sup>7</sup>G cap had a protective function against IFIT1, which was additive with the effect observed for the 2'-<i>O</i> position (m<sup>6</sup>A<sub>m</sub> cap-1). In contrast, an increased affinity for IFIT1 was observed for several noncanonical caps, including trimethylguanosine, unmethylated (G), and flavin-adenine dinucleotide caps. The results suggest new potential cellular targets of IFIT1 and may contribute to broadening the knowledge of the innate immune response mechanisms and the more effective design of chemically modified mRNAs.</p>","PeriodicalId":21401,"journal":{"name":"RNA","volume":" ","pages":"181-192"},"PeriodicalIF":4.2,"publicationDate":"2025-01-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11789485/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142792360","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
RNAPub Date : 2025-01-22DOI: 10.1261/rna.080254.124
Michael Anikin, Michael F Henry, Viktoria Hodorova, Hristo B Houbaviy, Jozef Nosek, Dimitri G Pestov, Dmitriy A Markov
{"title":"Mitochondrial mRNA and the small subunit rRNA in budding yeasts undergo 3'-end processing at conserved species-specific elements.","authors":"Michael Anikin, Michael F Henry, Viktoria Hodorova, Hristo B Houbaviy, Jozef Nosek, Dimitri G Pestov, Dmitriy A Markov","doi":"10.1261/rna.080254.124","DOIUrl":"10.1261/rna.080254.124","url":null,"abstract":"<p><p>Respiration in eukaryotes depends on mitochondrial protein synthesis, which is performed by organelle-specific ribosomes translating organelle-encoded mRNAs. Although RNA maturation and stability are central events controlling mitochondrial gene expression, many of the molecular details in this pathway remain elusive. These include <i>cis-</i> and <i>trans</i>-regulatory factors that generate and protect the 3' ends. Here, we mapped the 3' ends of mitochondrial mRNAs of yeasts classified into multiple families of the subphylum Saccharomycotina. We found that the processing of mitochondrial 15S rRNA and mRNAs involves species-specific sequence elements, which we term 3'-end RNA processing elements (3'-RPEs). In <i>Saccharomyces cerevisiae,</i> the 3'-RPE has long been recognized as a conserved dodecamer sequence, which recent studies have shown specifically interacts with the nuclear genome-encoded pentatricopeptide repeat protein Rmd9. We also demonstrate that, analogous to Rmd9 in <i>S. cerevisiae</i>, two Rmd9 orthologs from the <i>Debaryomycetaceae</i> family interact with their respective 3'-RPEs found in mRNAs and 15S rRNA. Thus, Rmd9-dependent processing of mitochondrial RNA precursors may be a common mechanism among the families of the Saccharomycotina subphylum. Surprisingly, we observed that 3'-RPEs often occur upstream of stop codons in complex I subunit mRNAs from yeasts of the CUG-Ser1 clade. We examined two of these mature mRNAs and found that their stop codons are indeed removed. Thus, translation of these stop-codon-less transcripts would require a noncanonical termination mechanism. Our findings highlight Rmd9 as a key evolutionarily conserved factor in both mitochondrial mRNA metabolism and mitoribosome biogenesis in a variety of yeasts.</p>","PeriodicalId":21401,"journal":{"name":"RNA","volume":" ","pages":"208-223"},"PeriodicalIF":4.2,"publicationDate":"2025-01-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11789488/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142688618","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}