Endoglucanase E, produced at high level in Escherichia coli as a lacZ′ fusion protein, is part of the Clostridium thermocellum cellulosome

• Published in: Enzyme and microbial technology Vol. 12; no. 9; pp. 656 - 662
• Main Authors: Hazlewood, Geoffrey P., Davidson, Keith, Clarke, Jonathan H., Durrant, Alastair J., Hall, Judith, Gilbert, Harry J.
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 01.09.1990
• Subjects: Amino Acid Sequence; Base Sequence; Cellulase - biosynthesis; Cellulase - genetics; Cellulase - secretion; cloning; Clostridium - enzymology; Clostridium - genetics; Clostridium thermocellum; DNA Mutational Analysis; Endoglucanase; endoglucanase E; Escherichia coli; Escherichia coli - metabolism; gene fusion; genes; Macromolecular Substances; Molecular Sequence Data; Molecular Weight; Protein Processing, Post-Translational; Protein Sorting Signals - physiology; Recombinant Fusion Proteins - biosynthesis; Recombinant Fusion Proteins - secretion; Structure-Activity Relationship; Subcellular Fractions - enzymology; Endoglucanase; Clostridium thermocellum; Escherichia coli

The Clostridium thermocellum celE gene was expressed at high level in Escherichia coli TG1 when placed under the transcriptional and translational control of lacZ′ in pUC18; in the presence of a multicopy plasmid (pNM52) containing the lacI q gene, expression of full-length and truncated forms of ce...