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Microbiology 143 (1997), 3185-3192; DOI  10.1099/00221287-143-10-3185
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Binding of colicins A and E1 to purified ToIA domains

Rahmona Derouiche1, Gabrielle Zeder-Lutz2, Hélène Bénédetti1, Marthe Gavioli1, Alain Rigal1, Claude Lazdunski1 and Roland LloubèAs1,1

Laboratoire d'Ingénierie et Dynamique des SystèAmes Membranaires, UPR 9027, Institut de Biologie Structurale et Microbiologic, 13402 Marseille Cedex 20, France
Laboratoire d'Immunochimie des Peptides et Virus, UPR 9021, 67084 Strasbourg Cedex, France

1 Author for correspondence: Roland Lloubès. Tel: +33 4 91 126 45 54. Fax: +33 4 91 71 21 24. e-mail: lloubes@ibsm.cnrs-mrs.fr

ABSTRACT

Colicins are divided into two groups according to the proteins required for their import into sensitive bacteria. The Tol and TonB pathways are involved in import of group A and group B colicins respectively. Because previous analyses have shown that colicin E1 and colicin A (two group A colicins) interact in vitro with the C-terminal domain of TolA (TolAIII) while colicin B (group B colicin) does not, attention was focused on these interactions with purified proteins. TolA has been described as a three-domain protein with an N-terminal inner-membrane anchor and a long periplasmic region formed by two domains (TolAII and TolAIII). TolAIII, TolAII and TolAII-III soluble domains with an N-terminal hexa-histidine extension were purified. The interactions of colicins with the purified TolA domains were analysed by overlay Western blotting, which indicated that both N-terminal domains of colicins A and E1 interacted with TolAIII, while a gel shift procedure detected no interaction with colicin E1. The binding kinetic values of the N-terminal domains of colicins A and E1 to TolAIII were estimated by surface plasmon resonance and were shown to be similar.

Keywords: Tol proteins, colicins, protein interactions




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Copyright © 1997 Society for General Microbiology.