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[Preprint]. 2023 Oct 19:2023.02.01.526536. Originally published 2023 Feb 1. [Version 3] doi: 10.1101/2023.02.01.526536

Fig. 5. Comparison of SHAPE reactivities when bound to wild-type Trm10 and Trm10-KRR variant reveals the tRNA conformational changes necessary for methylation.

Fig. 5.

A, Schematic of comparison being made between KRR-bound tRNA and Trm10-bound tRNA. B, Difference SHAPE reactivities between Trm10-bound and KRR-bound tRNAs mapped onto secondary (top) and tertiary (bottom) structures for (left to right): tRNAGly-GCC (substrate), tRNATrp-CCA (substrate), tRNAVal-UAC (partial substrate), tRNALeu-CAA (nonsubstrate), and tRNASer-UGA (nonsubstrate). Difference in reactivity for C, tRNAGly-GCC and D, tRNATrp-CCA mapped onto a model of the Trm10-tRNA complex, highlighting conformational changes necessary for methylation. The model of the Trm10-tRNA complex was generated using the structure of TRMT10C bound to pre-tRNA (PDB: 7ONU) and tRNAPhe (PDB: 6LVR), and is comprised of: the Trm10 C-terminal domain (PDB: 4JWJ; green), tRNA (white) and the N-terminal domain of TRMT10C (yellow). The color scale for difference in SHAPE reactivity (Trm10-bound minus KRR-bound tRNA) is shown in the bottom of panel A.