Incomplete activation of Escherichia coli hemolysin (HlyA) due to mutations in the 3' region of hlyC.

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.

journal_name

J Bacteriol

journal_title

Journal of bacteriology

authors

Guzmán-Verri C,García F,Arvidson S

doi

10.1128/jb.179.18.5959-5962.1997

subject

Has Abstract

pub_date

1997-09-01 00:00:00

pages

5959-62

issue

18

eissn

0021-9193

issn

1098-5530

journal_volume

179

pub_type

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