Open AccessProperties of C‐terminal truncated derivatives of the activator, StrR, of the streptomycin biosynthesis in Streptomyces griseus
Author(s) -
Thamm Sven,
Distler Jürgen
Publication year - 1997
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1997.tb10339.x
Subject(s) - streptomyces griseus , activator (genetics) , transcription (linguistics) , biology , streptomyces , biochemistry , genetics , gene , bacteria , linguistics , philosophy
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.