Secretion of Cellulomonas fimi exoglucanase by Escherichia coli.
A leader sequence of 41 amino acids (aa) has been proposed as the signal sequence for the exoglucanase (Exg) from Cellulomonas fimi. The ability of this 41-aa peptide to function as a leader sequence has been shown here by gene fusion experiments in Escherichia coli. A hybrid leader sequence containing C-terminal 37 aa of the leader peptide and N-terminal 6 aa of beta-galactosidase (beta Gal) directed export of the Exg into the periplasm of E. coli. In contrast, hybrid beta Gal-Exg proteins in which the leader sequence is not present are retained in the cytoplasm.
D000595:Amino Acid Sequence; D001483:Base Sequence; D003352:Corynebacterium / Q000201:enzymology / Q000235:genetics*; D004262:DNA Restriction Enzymes; D004926:Escherichia coli / Q000201:enzymology / Q000235:genetics*; D044643:Glucan 1,4-beta-Glucosidase; D005959:Glucosidases / Q000235:genetics*; D010957:Plasmids; D021382:Protein Sorting Signals / Q000235:genetics*; D001616:beta-Galactosidase / Q000235:genetics; D001617:beta-Glucosidase / Q000235:genetics*
D021382:Protein Sorting Signals; D004262:DNA Restriction Enzymes; D005959:Glucosidases; D001617:beta-Glucosidase; D001616:beta-Galactosidase; D044643:Glucan 1,4-beta-Glucosidase