Fig. 1: Sequence-dependent HJ cleavage by chloroplast MOC1s. | Nature Communications

Fig. 1: Sequence-dependent HJ cleavage by chloroplast MOC1s.

From: Structural insights into sequence-dependent Holliday junction resolution by the chloroplast resolvase MOC1

Fig. 1

a Schematic drawing of the HJ substrate X2. X2 was prepared by annealing 4 DNA oligos. The upper panel shows the structure of X2 (CCGG). Two homologous base pairs are shaded in gray. The lower panel indicates X2s with variant CCGG cores. These X2s share identical nucleotides as X2 (CCGG) except the 2 bp homologous cores. These seven X2s are numbered sequentially (I-VII). Arrows indicate the cleavage site. b The sequence-specific HJ resolution activity of MOC1 orthologs was examined. AtMOC1, GmMOC1, GrMOC1, NtMOC1, OsMOC1, and ZmMOC1 are MOC1s from Arabidopsis thaliana, Glycine max, Gossypium raimondii, Nicotiana tabacum, Oryza sativa, and Zea mays, respectively. The final HJ concentration in each lane is 250 nM. The final protein concentration of MOC1 is 1000 nM. The reactions were examined by native PAGE and visualized by GelRed staining. Labels on the top indicate the different X2 substrates used as shown in a. Source data are provided as a Source Data file.

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