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Figure 1 | Scientific Reports

Figure 1

From: Identification, heterologous production and bioactivity of lentinulin A and dendrothelin A, two natural variants of backbone N-methylated peptide macrocycle omphalotin A

Figure 1

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.

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