Correction to: Scientific Reports https://doi.org/10.1038/s41598-021-83106-2, published online 11 February 2021
The original version of this Article contained errors in Figures 1 and 2, where the methylation patterns of the peptide sequences were incorrect in Figure 1 panel (c) and Figure 2 panel (a). The original Figures 1 and 2 and accompanying legends appear below.
Structure and function of omphalotin biosynthetic gene cluster and homologous clusters in the basidiomycetes O. olearius, D. bispora and L. edodes. (A) Schematic representation of the borosin biosynthetic gene clusters in the basidiomycetes O. olearius (VT 653.13, scaffold_169), L. edodes (Le(Bin) 0899 ss11, scaffold_10) and D. bispora (CBS 962.96, scaffold_621). All three clusters code for a precursor (methyltransferase) protein, referred to as OphMA, LedMA and DbiMA1 respectively, and a prolyloligopeptidase, referred to as OphP, LedP and DbiP, respectively. The DNA scaffolds and filtered gene models were taken from https://mycocosm.jgi.doe.gov/. Double slashes (//) indicate that the sequence of the DNA scaffold continues beyond this position. (B) Biosynthesis scheme of omphalotin A and closely related peptides, lentinulin A and dendrothelin A as a combined action of the precursor (methyltransferase) protein and the prolyloligopeptidase. (C) Alignment of the C-termini of the precursor (methyltransferase) proteins from O. olearius (OphMA), L. edodes (LedMA) and D. bispora (DbiMA1). Residues differing from the omphalotin core peptide are shown in red. The indicated methylation patterns (green fill) were previously determined by heterologous expression of the respective cDNAs in E. coli21,23,25. CRS C-terminal recognition sequence.
Production of backbone N-methylated peptide macrocycles in P. pastoris. (A) Methylation pattern of OphMA, OphMA_LedCORE and OphMA_DbiCORE. Methylated residues were determined by LC–MS/MS analysis of the C-terminal tryptic fragments and are shaded in green (Supplementary Fig. S2A–C). (B) Production of omphalotin A. The extracted compound was detected using LC–MS and compared to the chemically synthesized omphalotin A standard (216 ng/ml). In addition to omphalotin A, fully methylated, linear (core) peptides and short linear peptides lacking the C-terminal three residues (VIG) were detected. (C) Production of lentinulin A and (D) dendrothelin A. The detected peptides were confirmed by LC–MS/MS. The confirmed positions of methylation are depicted using filled circles, while methylated residues inferred from MS/MS are shown in open circles. Residues different from omphalotin A are underlined. The mass difference (represented in ppm) between observed values and theoretical mass is indicated in brackets for each compound.
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Matabaro, E., Kaspar, H., Dahlin, P. et al. Author Correction: Identification, heterologous production and bioactivity of lentinulin A and dendrothelin A, two natural variants of backbone N-methylated peptide macrocycle omphalotin A. Sci Rep 12, 17021 (2022). https://doi.org/10.1038/s41598-022-21642-1
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DOI: https://doi.org/10.1038/s41598-022-21642-1

