Synthesis of the Streptomyces lividans maltodextrin ABC transporter depends on the presence of the regulator MalR

Autor(en): Schlosser, A
Weber, A
Schrempf, H 
Stichwörter: ABC transporter; CELLOBIOSE; COELICOLOR A3(2); CRYSTAL-STRUCTURE; ESCHERICHIA-COLI; GENE; glucose repression; LACI-GALR FAMILY; MalR repressor; MALTOSE-BINDING; maltose/maltodextrin; MEMBER; Microbiology; PROTEIN; Reg1 repressor; regulation of transcription; STREPTOCOCCUS-PNEUMONIAE; Streptomyces
Erscheinungsdatum: 2001
Herausgeber: ELSEVIER SCIENCE BV
Journal: FEMS MICROBIOLOGY LETTERS
Volumen: 196
Ausgabe: 1
Startseite: 77
Seitenende: 83
Zusammenfassung: 
During growth with maltotriose or amylose, Streptomyces lividans and Streptomyces coelicolor A3(2) synthesize a maltodextrin uptake system with highest specificity for maltotriose. The transport activity is absent in mutants of S. coelicolor A3(2) lacking a functional MalE binding protein. Cloning and sequencing data suggest that the mal operon of S. coelicolor A3(2) corresponds to the one of S. lividans and that the deduced S. lividans Reg1 amino acid sequence is identical to that of MalR from S. coelicolor A3(2). It can be concluded that both strains have the same ABC transport system for maltodextrins. The S. lividans malR was cloned in Escherichia coli in frame with six histidine-encoding codons. The resulting, purified 6HisMalR(Sl) was shown to bind to two motifs within the S. lividans malR-malE intergenic region and to dissociate in the presence of maltopentaose. (C) 2001 Federation of European Microbiological Societies. Published by Elsevier Science B.V. All rights reserved.
ISSN: 03781097
DOI: 10.1111/j.1574-6968.2001.tb10544.x

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