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PMID: 6325242 Published · ppublish English Comparative Study Journal Article Research Support, Non-U.S. Gov't

Evolution and structure of two ADP-ribosylation enterotoxins, Escherichia coli heat-labile toxin and cholera toxin.

FEBS letters ·Vol. 169 ·No. 2 ·1984-04-24 ·Pages 241-6

Yamamoto T, Nakazawa T, Miyata T, Kaji A, Yokota T

Abstract

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 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.

MeSH Terms
Amino Acid Sequence Bacterial Toxins/genetics Base Sequence Cholera Toxin/genetics Enterotoxins/genetics Escherichia coli Escherichia coli Proteins Models, Molecular Nucleotidyltransferases/metabolism Operon Poly(ADP-ribose) Polymerases
Chemicals
Bacterial Toxins Enterotoxins Escherichia coli Proteins heat-labile enterotoxin, E coli Cholera Toxin Poly(ADP-ribose) Polymerases Nucleotidyltransferases
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Yamamoto T
Nakazawa T
Miyata T
Kaji A
Yokota T
Article Info
Journal
FEBS letters
Abbr.
FEBS Lett
ISSN
0014-5793
Published
1984-04-24
Pages
241-6
Language
English
Region
England
NLM ID
0155157
Subset
IM
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