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

Autor(en): Schlosser, A
Aldekamp, T
Schrempf, H 
Stichwörter: actinomycete; CebR regulator; CELLOBIOSE; cellobiose/cellatriose ABC transporter; CELLULASE AVICELASE; COMPONENT; CRYSTAL-STRUCTURE; DNA; GENES; Microbiology; PROTEIN; streptomycete; TRANSPORT-SYSTEM
Erscheinungsdatum: 2000
Herausgeber: ELSEVIER SCIENCE BV
Journal: FEMS MICROBIOLOGY LETTERS
Volumen: 190
Ausgabe: 1
Startseite: 127
Seitenende: 132
Zusammenfassung: 
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. (C) 2000 Federation of European Microbiological Societies. Published by Elsevier Science B.V. All rights reserved.
ISSN: 03781097
DOI: 10.1016/S0378-1097(00)00304-9

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