PMID:9294460
| Citation |
Guzmán-Verri, C, García, F and Arvidson, S (1997) Incomplete activation of Escherichia coli hemolysin (HlyA) due to mutations in the 3' region of hlyC. J. Bacteriol. 179:5959-62 |
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| Abstract |
Mutational analysis of the carboxy-terminal region of Escherichia coli HlyC was performed by site-directed mutagenesis. Replacement of residue Val-127 or Lys-129 reduced the activity of HlyC to about 30 or 60%, respectively, of that of the wild type, while replacement of Gly-128 reduced the activity to less than 1% of the wild-type level. Complete inactivation of HlyC was caused by a double mutation, replacement of Gly-128 with valine and of Lys-129 with isoleucine. Analysis of culture supernatants from mutants with reduced hemolytic activity by two-dimensional gel electrophoresis revealed the production and simultaneous secretion of nonacylated, monoacylated, and fully acylated HlyA forms, demonstrating impairment of the acylation reaction, possibly due to a decreased affinity of HlyC for the individual HlyA acylation sites. |
| Links | |
| Keywords |
Acylation; Acyltransferases; Amino Acid Sequence; Bacterial Proteins/genetics; Bacterial Proteins/metabolism; Electrophoresis, Gel, Two-Dimensional; Escherichia coli/genetics; Escherichia coli/metabolism; Escherichia coli/pathogenicity; Escherichia coli Proteins; Gene Expression Regulation, Bacterial; Hemolysin Proteins/genetics; Hemolysin Proteins/metabolism; Macromolecular Substances; Molecular Sequence Data; Point Mutation; Structure-Activity Relationship |
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