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Structural and genomic DNA analysis of the putative TetR transcriptional repressor SCO7518 from Streptomyces coelicolor A3(2)
Author(s) -
Hayashi Takeshi,
Tanaka Yoshikazu,
Sakai Naoki,
Okada Ui,
Yao Min,
Watanabe Nobuhisa,
Tamura Tomohiro,
Tanaka Isao
Publication year - 2014
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2014.09.037
Subject(s) - tetr , streptomyces coelicolor , repressor , electrophoretic mobility shift assay , biology , dna , genomic dna , gene , genetics , dna binding domain , transcriptional regulation , microbiology and biotechnology , gene expression , transcription factor , mutant
SCO7518 is a protein of unknown function from Streptomyces coelicolor A3(2) that has been classified into the TetR transcriptional regulator family. In this study, a crystal structure of SCO7518 was determined at 2.29 Å resolution. The structure is a homodimer of protomers that comprise an N‐terminal DNA‐binding domain and a C‐terminal dimerization and regulatory domain, and possess a putative ligand‐binding cavity. Genomic systematic evolution of ligands by exponential enrichment and electrophoretic mobility shift assays revealed that SCO7518 specifically binds to an operator sequence located upstream of the sco7519 gene, which encodes a maltose O‐acetyltransferase. These results suggest that SCO7518 is a transcriptional repressor of sco7519 expression.