Journal of Bacteriology, November 2001, p. 6721-6725, Vol. 183, No. 22
Laboratoire d'Ingénierie des
Systèmes Macromoléculaires, Institut de Biologie
Structurale et Microbiologie, CNRS, 13402 Marseille cedex 20, France
Received 5 March 2001/Accepted 23 August 2001
The colicin A pore-forming domain (pfColA) was fused to a bacterial
signal peptide (sp-pfColA). This was inserted into the Escherichia coli inner membrane in functional form and
could be coimmunoprecipitated with epitope-tagged immunity protein
(EpCai). We constructed a series of fusion proteins in which various
numbers of sp-pfColA
0021-9193/01/$04.00+0 DOI: 10.1128/JB.183.22.6721-6725.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.
Colicin A Immunity Protein Interacts with the
Hydrophobic Helical Hairpin of the Colicin A Channel Domain in the
Escherichia coli Inner Membrane
-helices were fused to alkaline phosphatase
(AP). We showed that a fusion protein made up of the hydrophobic
-helices 8 and 9 of sp-pfColA fused to AP was specifically
coimmunoprecipitated with EpCai produced in the same cells. This is the
first biochemical evidence that Cai recognizes and interacts with the
colicin A hydrophobic helical hairpin.
*
Corresponding author. Mailing address: Laboratoire
d'Ingénierie des Systèmes Macromoléculaires,
Institut de Biologie Structurale et Microbiologie, CNRS, 31 chemin
Joseph Aiguier, 13402 Marseille cedex 20, France. Phone: 33 04 91 16 45 61. Fax: 33 04 91 71 21 24. E-mail:
duche{at}ibsm.cnrs-mrs.fr.
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