Fig. 1: pre-tRNA 5’-end processing and folding of HARPs.
A Domain architectures of PRORPs. B In vitro pre-tRNAGly cleavage assays catalyzed by different HARPs. The substrate cleavage percentage (%) is shown at the bottom of the gels. Experiments were repeated independently twice with similar results. Source data are provided in Source Data file. C, D Cartoon and surface presentation showing the folding of PbHARP AB dimer observed in the apo-form structure. E Cartoon presentation of the apo-form TcHARP structure. F Structural superposition of PbHARP and TcHARP. The PbHARP AB dimer is colored as in panel (C), the TcHARP dimer is colored as in panel (E). G H-bond interactions involved in PbHARP dimerization in the apo-form structure. H Structural superposition showing the conformational difference between the HB domains of PbHARP A and B monomers. In panels (G), (H), the C-atoms are colored in yellow and cyan in the A and B monomers, respectively.
