Details

Autor(en) / Beteiligte

• Kheng B. Lim
• Carthene R. Bazemore Walker
• Lin Guo
• Shahaireen Pellett
• Jeffrey Shabanowitz
• Donald F. Hunt
• Erik L. Hewlett
• Albrecht Ludwig
• Werner Goebel
• Rodney A. Welch
• Murray Hackett

Titel

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 .