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N‐terminus of mature heat‐labile enterotoxin chain B is critical for its extracellular secretion in Vibrio cholerae
Author(s) -
Mukhija Reema,
Garg Lalit C
Publication year - 1999
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(99)01504-5
Subject(s) - periplasmic space , vibrio cholerae , secretion , enterotoxin , extracellular , escherichia coli , biochemistry , biology , secretory protein , n terminus , chemistry , microbiology and biotechnology , bacteria , peptide sequence , genetics , gene
The effects of addition of a few amino acids to the amino‐ and carboxy‐terminal regions of the mature portion of the heat‐labile enterotoxin chain B (LTB) of Escherichia coli on protein export, secretion and assembly were investigated. In E. coli , LTB (secretory protein) with or without the extension at the N‐ or C‐terminus accumulated in the periplasmic fraction. For Vibrio cholerae , LTB with the extension at the C‐terminus was exported to the periplasm followed by secretion to the extracellular milieu. However, LTB with the N‐terminus extension was exported to the periplasm only. Our findings suggest that in the case of V. cholerae , the N‐terminus of the mature LTB plays an important role in its secretion to the extracellular milieu.