Site-directed mutagenesis of the hole-forming toxin aerolysin: studies on the roles of histidines in receptor binding and oligomerization of the monomer.

doi:10.1021/bi00460a031

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Article

Site-directed mutagenesis of the hole-forming toxin aerolysin: studies on the roles of histidines in receptor binding and oligomerization of the monomer.

Biochemistry - 27 Feb 1990

Green M J, Buckley J T

Abstract excerpt

The six histidines of the channel-forming protein aerolysin have been replaced one at a time with asparagine by site-directed mutagenesis, and each of the modified proteins has been purified. Three proteins had the same hemolytic activity as native toxin, but the others, those changed at His107,...

Topics

Aeromonas
Animals
Bacterial Toxins
Base Sequence
Erythrocytes
Escherichia coli
Hemolysis
Histidine
Humans
Molecular Sequence Data
Mutation
Plasmids
Pore Forming Cytotoxic Proteins
Rats
Receptors, Cell Surface

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