Abstract
The regulatory protein Reg1 of Streptomyces lividans (a member of the LacI family) was expressed in Escherichia coli as a translational fusion with the maltose-binding protein (MBP) of E. coli. The purified MBP-Reg1 binds the promoter region of genes of the maltose regulon (amylases, maltose utilization) and that of genes sensitive to catabolite repression (chitinase, xylanase, cellulase). Repeated sequences, in direct or inverted orientation, are involved in these DNA-protein interactions. They are present in all DNA fragments able to bind MBP-Reg1. The nucleotide sequence of the repeats and the variability of the spacing between them suggest a similarity in DNA-binding activity between Reg1 and CytR, another member of the LacI family.

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