The images for Figs 7 and 8 are incorrectly switched. The image that appears as Fig 7 should be Fig 8, and the image that appears as Fig 8 should be Fig 7. The figure captions appear in the correct order. Please see the corrected Fig 7 here.
Fig 7. Amino acid residues alignment of CamCPR, caa_locus_6894, caa_locus_12198, and caa_locus_112450 using Clustal Omega multiple aligment tool.
The identical amino acid residues between CamCPR and caa_locus_6894 were highlighted in red, between CamCPR and caa_locus_12198 were in green, and between CamCPR and caa_locus_112450 were in blue.
Fig 8. Enzymatic digestion and chemical degradation of tCamCPR.
The predicted cleavage sites of tCamCPR (a) and the detected peptide fragments by SDS-PAGE analysis (b). T, thrombin; H, Hydroxylamine; M, protein ruler; Lane 1, tCamCPR; Lane 2, thrombin; Enzyme digestion products of tCamCPR with 1 U / 50 μL (Lane 3) and 2 U / 50 μL (Lane 4) of thrombin were used [37]; Lanes 5 and 6, chemical degradation products of tCamCPR by hydroxylamine [38].
Please see the corrected Fig 8 here.
Reference
- 1. Qu X, Pu X, Chen F, Yang Y, Yang L, Zhang G, et al. (2015) Molecular Cloning, Heterologous Expression, and Functional Characterization of an NADPH-Cytochrome P450 Reductase Gene from Camptotheca acuminata, a Camptothecin-Producing Plant. PLoS ONE 10(8): e0135397 doi: 10.1371/journal.pone.0135397 [DOI] [PMC free article] [PubMed] [Google Scholar]


