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Ecm16 protein confers resistance against the DNA intercalator antibiotic echinomycin
Author(s) -
Gade Priyanka,
Erlandson Amanda,
Mathews Irimpan I.,
Chen Xi,
Mera Paola,
Kim ChuYoung
Publication year - 2021
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.2021.35.s1.03214
Subject(s) - dna , chemistry , gene , microbiology and biotechnology , nucleotide , biochemistry , biology
Echinomycin is a nonribosomal peptide antibiotic that acts by intercalating double‐stranded DNA . The echinomycin biosynthetic gene cluster of Streptomyces lasaliensis contains a gene of unverified function, ecm16 . We show that expression of Ecm16 in the echinomycin‐sensitive E. coli K12 renders cells resistant to echinomycin. Additionally, we have determined the X‐ray crystal structure of Ecm16 at 2.0 Å resolution. Interestingly, the three‐dimensional structure of Ecm16 resembles that of UvrA, the DNA damage sensor protein from the prokaryotic nucleotide excision repair pathway. Ecm16, like UvrA, contains two nucleotide binding domains on a single polypeptide chain, and it can bind double‐stranded DNA. However, our results show that neither UvrA nor Ecm16 can complement each other's function in vivo .