PMID:8576066
| Citation |
Chervaux, C and Holland, IB (1996) 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. J. Bacteriol. 178:1232-6 |
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| 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. |
| Links | |
| Keywords |
Amino Acid Sequence; Bacterial Proteins/genetics; Bacterial Proteins/physiology; DNA Mutational Analysis; Escherichia coli/genetics; Escherichia coli/metabolism; Escherichia coli Proteins; Hemolysin Proteins/genetics; Hemolysin Proteins/physiology; Molecular Sequence Data; Mutagenesis; Protein Structure, Secondary; Structure-Activity Relationship |
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