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• W1536061423 abstract "The HlyA secretion signal sequence of approximately 46 residues is predicted to contain helix I and an amphipathic helix II separated by a short loop including the conserved Phe residue, F-989. All nine substitutions of Phe-989 drastically reduce secretion of HlyA. Directed mutagenesis identified a functional hot spot, EISK, in helix II. However, genetic analysis did not provide strong support for a functional helix II; rather, the results emphasized that individual residues, for example, E-978 and F-989, are essential irrespective of a specific secondary structure." @default.
• W1536061423 created "2016-06-24" @default.
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• W1536061423 date "1996-02-01" @default.
• W1536061423 modified "2023-09-24" @default.
• W1536061423 title "Random and directed mutagenesis to elucidate the functional importance of helix II and F-989 in the C-terminal secretion signal of Escherichia coli hemolysin" @default.
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• W1536061423 doi "https://doi.org/10.1128/jb.178.4.1232-1236.1996" @default.
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