Properties of C-terminal truncated derivatives of the activator, StrR, of the streptomycin biosynthesis in Streptomyces griseus

• Published in: FEMS microbiology letters Vol. 149; no. 2; pp. 265 - 272
• Main Authors: Thamm, Sven, Distler, Jürgen
• Format: Journal Article
• Language: English
• Published: Oxford, UK Blackwell Publishing Ltd 01.04.1997; Oxford University Press
• Subjects: Activator; Amino Acid Sequence; Amino acids; Bacterial Proteins - chemistry; Bacterial Proteins - genetics; Bacterial Proteins - metabolism; Binding sites; Biosynthesis; Deoxyribonucleic acid; DNA; DNA-binding protein; DNA-Binding Proteins - chemistry; DNA-Binding Proteins - genetics; DNA-Binding Proteins - metabolism; Electrophoresis, Polyacrylamide Gel; Escherichia coli - genetics; Escherichia coli - metabolism; Gene Expression Regulation, Bacterial - physiology; Helix-Loop-Helix Motifs - genetics; Microbiology; Molecular Sequence Data; Mutagenesis - physiology; Plasmids; Protein Binding - physiology; Protein Structure, Tertiary; Proteins; Streptomyces griseus; Streptomyces griseus - metabolism; Streptomycin; Streptomycin - biosynthesis; Transcription; Transcription Factors - chemistry; Transcription Factors - genetics; Transcription Factors - metabolism; Streptomycin biosynthesis; DNA-binding protein; Transcription; Activator
• ISSN: 0378-1097; 1574-6968
• DOI: 10.1111/j.1574-6968.1997.tb10339.x

Abstract The StrR protein is a DNA-binding protein activating the transcription of streptomycin biosynthesis of Streptomyces griseus N2-3-11 and Streptomyces glaucescens. A putative helix–turn–helix motif located between amino acid positions 207 and 227 of the StrR protein was identified as a prerequisite for its DNA-binding properties. Although, C-terminal truncated StrR proteins were able to interact with StrR-binding sites, they failed to activate transcription from the StrR-dependent promotor strB1p. Therefore, the C-terminal domain of StrR seemed to be necessary for its function as transcriptional activator.