A lipid-anchored binding protein is a component of an ATP-dependent cellobiose/cellotriose-transport system from the cellulose degrader Streptomyces reticuli

Autor(en): Schlosser, A
Schrempf, H 
Stichwörter: ACTIVE-TRANSPORT; BACILLUS-SUBTILIS; BACTERIAL PERIPLASMIC PERMEASES; Biochemistry & Molecular Biology; CELLOBIOSE UPTAKE; cellobiose/cellotriose transport; ESCHERICHIA-COLI; GRAM-POSITIVE BACTERIA; lipoprotein; PHOSPHOTRANSFERASE SYSTEM; STREPTOCOCCUS-MUTANS; Streptomyces reticuli; SUGAR-TRANSPORT; TRYPTOPHAN RESIDUES; uptake of glucose; vesicle
Erscheinungsdatum: 1996
Herausgeber: SPRINGER VERLAG
Journal: EUROPEAN JOURNAL OF BIOCHEMISTRY
Volumen: 242
Ausgabe: 2
Startseite: 332
Seitenende: 338
Zusammenfassung: 
During cultivation in the presence of cellobiose or crystalline cellulose, Streptomyces reticuli expresses an inducible uptake system that transports cellobiose (K-m, 4 mu-M), cellotriose and, to a lesser degree, cellotetraose and cellopentaose. Cellobiose uptake is dependent on ATP and inhibited by N-ethylmaleimide. A binding protein was identified in its palmitylated form in the cytoplasmic membrane of mycelia. It could be extracted with the detergent Triton X-100 and purified by two subsequent anion-exchange chromatographies. It showed highest affinity (K-d, 1.5 mu M) for cellobiose and cellotriose. The data suggest that cellobiose/cellotriose uptake is mediated by a membrane-anchored lipoprotein as a component of an ATP-binding-cassette-transporter system.
ISSN: 00142956
DOI: 10.1111/j.1432-1033.1996.0332r.x

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