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Front Cover: Biosynthetic Gene Cluster of a d ‐Tryptophan‐Containing Lasso Peptide, MS‐271 (ChemBioChem 19/2018)
Author(s) -
Feng Zhi,
Ogasawara Yasushi,
Nomura Satoshi,
Dairi Tohru
Publication year - 2018
Publication title -
chembiochem
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201800544
Subject(s) - gene cluster , peptide , gene , peptide biosynthesis , biology , streptomyces , biochemistry , asparagine , tryptophan synthase , heterologous expression , asparagine synthetase , chemistry , genetics , amino acid , rna , ribosome , recombinant dna , escherichia coli , bacteria
The front cover picture shows the biosynthesis of a d ‐tryptophan‐containing lasso peptide, MS‐271 produced by Streptomyces sp. M‐271. The MS‐271 biosynthetic gene cluster was identified by draft genome sequencing. We revealed that MS‐271 is a ribosomal peptide and that the d ‐Trp residue is introduced by epimerization of the precursor peptide. Besides the gene for the precursor peptide (MslA), the cluster contained genes encoding enzymes for post‐translational modifications such as an asparagine synthetase (MslC), a precursor peptide recognition element (MslB1), cysteine protease (MslB2), disulfide oxidoreductases (MslE, MslF), and a protein of unknown function (MslH). Although no obvious epimerase gene was present in the cluster, heterologous expression of the putative MS‐271 cluster in Streptomyces lividans showed that it contains all the necessary genes for MS‐271 production, including a gene for a new peptide epimerase. More information can be found in the communication by Y. Ogasawara, T. Dairi, et al. on page 2045 in Issue 19, 2018 (DOI: 10.1002/cbic.201800315).