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Escherichia coli α-Hemolysin (HlyA) Is Heterogeneously Acylated in Vivo with 14-, 15-, and 17-Carbon Fatty Acids
Ist Teil von
The Journal of biological chemistry, 2000-11, Vol.275 (47), p.36698
Ort / Verlag
American Society for Biochemistry and Molecular Biology
Erscheinungsjahr
2000
Quelle
Alma/SFX Local Collection
Beschreibungen/Notizen
α-Hemolysin (HlyA) is a secreted protein virulence factor observed in certain uropathogenic strains of Escherichia coli . The active, mature form of HlyA is produced by posttranslational modification of the protoxin that is mediated by acyl carrier
protein and an acyltransferase, HlyC. We have now shown using mass spectrometry that these modifications, when observed in
protein isolated in vivo , consist of acylation at the ε-amino groups of two internal lysine residues, at positions 564 and 690, with saturated 14-
(68%), 15- (26%), and 17- (6%) carbon amide-linked side chains. Thus, HlyA activated in vivo consists of a heterogeneous family of up to nine different covalent structures, and the substrate specificity of the HlyC
acyltransferase appears to differ from that of the closely related CyaC acyltransferase expressed by Bordetella pertussis .
Sprache
Englisch
Identifikatoren
ISSN: 0021-9258
eISSN: 1083-351X
DOI: 10.1074/jbc.C000544200
Titel-ID: cdi_highwire_biochem_275_47_36698
Format
–
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