Publication Date:
1994-12-23
Description:
Hemolysin of Escherichia coli is activated by fatty acylation of the protoxin, directed by the putative acyl transferase HlyC and by acyl carrier protein (ACP). Mass spectrometry and Edman degradation of proteolytic products from mature toxin activated in vitro with tritium-labeled acylACP revealed two fatty-acylated internal lysine residues, lysine 564 and lysine 690. Resistance of the acylation to chemical treatments suggested that fatty acid was amide linked. Substitution of the two lysines confirmed that they were the only sites of acylation and showed that although each was acylated in the absence of the other, both sites were required for in vivo toxin activity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stanley, P -- Packman, L C -- Koronakis, V -- Hughes, C -- New York, N.Y. -- Science. 1994 Dec 23;266(5193):1992-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pathology, Cambridge University, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7801126" target="_blank"〉PubMed〈/a〉
Keywords:
Acyl Carrier Protein/metabolism
;
Acylation
;
Acyltransferases/metabolism
;
Amino Acid Sequence
;
Animals
;
Bacterial Proteins/chemistry/metabolism/*toxicity
;
Bacterial Toxins/chemistry/metabolism/*toxicity
;
*Escherichia coli
;
*Escherichia coli Proteins
;
Hemolysin Proteins/chemistry/metabolism/*toxicity
;
Hemolysis
;
Horses
;
Lysine/metabolism
;
Mass Spectrometry
;
Molecular Sequence Data
;
Protein Precursors/metabolism
;
Sequence Alignment
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
Permalink