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Reinsch, J. L.

Publications and source records attributed to Reinsch, J. L..

3 recordsLinked to original sources

Pseudouridylation landscape across 42 S. cerevisiae cytosolic tRNA isoacceptors via Nanopore direct RNA sequencing

Pseudouridine is the most abundant RNA base modification due to its prevalence in tRNA and rRNA, where it serves as a key modulator of structure and function. Yet, in the widely used model organism, the budding yeast Saccharomyces cerevisiae, tRNA pseudouridine sites have not been comprehensively annotated. Here, we performed two high-throughput methods established for detecting tRNA pseudouridylation positions: Nanopore direct RNA sequencing (DRS) and 2-bromoacrylamide-assisted cyclization sequencing (BACS). Using DRS, we sequenced cytosolic tRNA from seven pseudouridine synthase (PUS) knockout S. cerevisiae strains, including deletion strains of Pus1, Pus3, and Pus7. Analysis of these data verified thirty-two existing pseudouridine annotations and predicted an additional ten previously unannotated pseudouridine sites. Our analysis also revealed DRS signal changes at several non-uridine sites with the loss of a PUS, including apparent changes in modification abundances at position 37 upon deletion of Pus3. Liquid chromatography tandem mass spectrometry (LC-MS/MS) and primer extension assays, however, indicated no change in the abundance of these modifications with the loss of Pus3, underscoring the need for caution in interpreting DRS-based signal changes. Using BACS, we confirmed the ten DRS-predicted novel sites, while further detecting eleven additional previously unannotated pseudouridine sites. Combining existing modification annotations from the Modomics database with our DRS and BACS datasets, we created a map of all detected pseudouridines --totaling 126 sites, including 21 novel sites--and the enzymes responsible for their catalysis, across the forty-two nuclear-encoded S. cerevisiae tRNA isoacceptors.

molecular biology↗

tRNA isodecoder analysis using Nanopore ionic current signals and deep learning

tRNA are short non-coding RNA characterized by their distinct tertiary structure and abundant chemical modifications. Conventional analysis strategies do not fully characterize tRNA isodecoders. We demonstrate that this limitation can be resolved for tRNA using nanopore ionic current data. We developed tRNAZAP, a deep learning strategy that uses nanopore ionic current signal information to classify native tRNA strands at isodecoder-level resolution without relying on sequence information. Additionally, the ionic current level classification allows for pairwise alignment of read sequences to reference sequences, producing optimal tRNA alignments. We applied tRNAZAP to direct tRNA sequencing data from Escherichia coli and Saccharomyces cerevisiae, and recovered 2.6% and 13.1% more aligned reads than BWA-MEM, respectively. tRNAZAP resolved these reads at an isodecoder-level and with consistently higher alignment identity. tRNAZAP is a powerful complement to sequence-based profiling and can contribute towards resolving the isodecoder landscape in more complex organisms including humans.

genomics↗

Concurrent detection of chemically modified bases in yeast mitochondrial tRNAs by Nanopore direct RNA sequencing

Saccharomyces cerevisiae is an invaluable model in the study of mitochondrial tRNA biology. Yet the positions of modified bases in all yeast mitochondrially-encoded tRNAs (mt-tRNAs) are still not fully mapped. We performed Nanopore direct RNA sequencing (DRS) on tRNAs from the crude mitochondrial fraction of yeast to map base modifications across all 24 mt-tRNA isoacceptors. Additionally, we developed a method to detect dihydrouridine sites in tRNAs, tD-seq, where chemical reduction of dihydrouridine causes disruptions to reverse transcription. We mapped dihydrouridine, pseudouridine, and N2-dimethylguanosine sites in mt-tRNAs using DRS, tD-seq, and knockouts of five conserved tRNA-modifying enzymes. Our results establish Dus1 and Dus2 as the enzymes responsible for D14, D16, D17, D17a, and D20 formation in S. cerevisiae mt-tRNAs, and revealed interactions between Dus1, Dus2, and Trm1-catalyzed modifications. We provide a comprehensive analysis of S. cerevisiae mt-tRNA base modifications, and identify novel modification "circuits" in yeast mt-tRNAs, in which the loss of a single enzymes activity can change modification levels at sites catalyzed by other enzymes. These findings expand our understanding of mt-tRNA base modifications and their interdependence, and advance opportunities for the yeast model for investigating defects in human mt-tRNA function. GRAPHICAL ABSTRACT O_FIG O_LINKSMALLFIG WIDTH=200 HEIGHT=80 SRC="FIGDIR/small/653160v2_ufig1.gif" ALT="Figure 1"> View larger version (27K): org.highwire.dtl.DTLVardef@9b7315org.highwire.dtl.DTLVardef@1a089dcorg.highwire.dtl.DTLVardef@bb01b7org.highwire.dtl.DTLVardef@16dd34d_HPS_FORMAT_FIGEXP M_FIG C_FIG

molecular biology↗