Binding characteristics of CebR, the regulator of the ceb operon required for cellobiose/cellotriose uptake in Streptomyces reticuli

1 September 2000

journal article
Published by Oxford University Press (OUP) in FEMS Microbiology Letters

Vol. 190 (1) , 127-132
https://doi.org/10.1016/s0378-1097(00)00304-9

Abstract

The Streptomyces reticuli Avicelase (cellulase, Cell) hydrolyzes crystalline cellulose to cellooligomers, cellobiose and cellotriose which are taken up by mycelia via an ABC transport system (Ceb) induced during growth with cellobiose or cellulose. The cebR gene located upstream of the cebEFG operon was cloned in Escherichia coli in frame with six histidine-encoding codons. The resulting purified fusion protein was shown to bind to a motif of 23 bp, including a perfect 18-bp palindrome situated upstream of the cebEFG. Cytoplasmic extracts of induced, but not of uninduced S. reticuli protected the same DNA motif. Release of the CebR regulator from its operator occurs upon addition of cellopentaose which can be assumed to act as inducer within the mycelia.

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