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Evolution and structure of two ADP‐ribosylation enterotoxins, Escherichia coli heat‐labile toxin and cholera toxin
Author(s) -
Yamamoto Tatsuo,
Nakazawa Teruko,
Miyata Takashi,
Kaji Akira,
Yokota Takeshi
Publication year - 1984
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 - 10.1016/0014-5793(84)80326-9
Subject(s) - cholera toxin , enterotoxin , toxin , escherichia coli , adp ribosylation , heat labile enterotoxin , biology , gene , vibrio cholerae , nucleotide , heat stable enterotoxin , microbiology and biotechnology , chemistry , biochemistry , genetics , enzyme , bacteria , nad+ kinase
Nucleotide sequence comparisons of the heat‐labile enterotoxin (LTh) genes of E. coli pathogenic for humans with cholera toxin (CT) genes suggest that the two toxin genes have evolved from a common ancestry by a series of single selective base changes, while conserving the catalytic fragment A1 (ADP‐ribose transferase). Based on the local hydrophilicity profiles of LTh and CT peptides, a transmembrane segment appears to be present in A1 in both toxins.