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Image Search Results
Journal: Clinical and Translational Medicine
Article Title: The m 5 C methyltransferase NSUN2 promotes codon‐dependent oncogenic translation by stabilising tRNA in anaplastic thyroid cancer
doi: 10.1002/ctm2.1466
Figure Lengend Snippet: The deletion of cytoplasmic tRNA methylation induced by NSUN2 knockdown showed a species bias and secondary structure bias, and led to a decrease in the overall protein translation level. (A and B) LC–MS analysis of total 5‐methylcytidine (m 5 C) levels in purified tRNA from vector (A) and shN (B) cells. (C) Heatmap of m 5 C‐modified cytoplasmic tRNAs in the NSUN2 knockdown and control cells. Each cell shows the summarised m 5 C level of a representative tRNA isodecoder. The colour represents the relative intensity of methylation changes. (D) Heatmap illustrating the methylation levels of different cytosines on candidate tRNAs, as determined by bisulphite sequencing of tRNA preparations from the NSUN2 knockdown and control cells. A gradient from green to red indicates the methylation rate from 0 to 100%. (E) Quantification of m 5 C level on m 5 C‐modified tRNAs. (F) Motif sequence at m 5 C sites, p value < .001, E value < 0.01. (G) Ridge plot showing the change of m 5 C methylation rate density on tRNA secondary structure between vector and shN cells. Each short vertical line represents methylation rate of a specific m 5 C site. (H) The effects of NSUN2 knockdown and expression on protein synthesis in KHM‐5 M, BHT‐101 and 8305C as analysed by puromycin intake assay. (I) Statistical analysis on the basis of puromycin incorporation to monitor protein synthesis. Data are shown as mean ± SD of N = 3 biological replicates. (J) Human genome mature tRNA Leu‐CAA and CAG, the green part indicates that there are detectable m 5 C modification sites on the tRNA sequence.
Article Snippet:
Techniques: Methylation, Knockdown, Liquid Chromatography with Mass Spectroscopy, Purification, Plasmid Preparation, Modification, Control, Bisulfite Sequencing, Sequencing, Expressing
Journal: Clinical and Translational Medicine
Article Title: The m 5 C methyltransferase NSUN2 promotes codon‐dependent oncogenic translation by stabilising tRNA in anaplastic thyroid cancer
doi: 10.1002/ctm2.1466
Figure Lengend Snippet: Depletion of NSUN2‐mediated m5C caused a decrease in tRNA and an increase in cleaved fragments. (A) A method for tRNA charging assay. (B) tRNA charging level of indicated isodecoder family was measured. Primers specific to Leu‐CAA and Leu‐CAG were used. (C) qRT‐PCR analysis of tRNA Leu‐CAA. (D) Relationship of tRNA related RNA fragments. (E) qRT‐PCR analysis of tRNA Leu related RNA fragments. (F) Correlation scatter plot showing that tRNA expression is positively associated with m 5 C modification at variable loop. (G) Comparison between tRNA Leu‐CAA isodecoders expression and m 5 C modification. The bubble size represents the proportion of tRNA Leu‐CAA isodecoders in vector cell. (H) Comparison between tRNA expression and m 5 C modification at variable loop. Each row represents the same tRNA isodecoder. (I) The 3D structure diagram shows the position of C48 (green dot) and TΨC loop/arm (red shaded part) in tRNA Leu‐CAA‐2‐1. The blue, red, white orange and grey sphere represents the nitrogen atom ( N ), oxygen atom ( O ), hydrogen atom ( H ), phosphorus atom ( P ) and the carbon atom ( C ). In the secondary structure of tRNA Leu‐CAA, short red line indicates the possible cleavage sites of tRNA after methylation deletion. (J) Working model for NSUN2 mediated tRNA m 5 C modification in regulation of ATC tumourigenesis. NSUN2 sustains tRNA stability by catalysing m 5 C modification and enhances translation in cancer.
Article Snippet:
Techniques: Quantitative RT-PCR, Expressing, Modification, Comparison, Plasmid Preparation, Methylation