Both colicin A and colicin Ia belong to a subfamily of the bacterial colicins that act by forming a voltage-dependent channel in the inner membrane of target bacteria. Both colicin A and Ia open at positive and close at negative potential, but only colicin A exhibits distinctly biphasic turnoff kinetics, implying the existence of two open states. Previous work has shown that Colicin Ia gating is associated with the translocation of a region representing 4 of its alpha helices across the membrane. Also, if its C-terminal, channel-forming domain is detached from the other domains, its N-terminal alpha helix can now also cross the membrane, causing the conductance to drop by a factor of about 6. Colicin A gating also involves the translocation of an internal domain, but we find that its translocated domain is somewhat smaller than that of Ia. Furthermore, while its isolated C-terminal domain can also undergo a transition to a smaller conductance, the conductance change is only about 15%, and the transition does not involve the translocation of the N-terminal alpha helix. Trapping the N-terminus on the cis side prevents neither this small conductance transition nor the biphasic turn-off. So, while the gating of both channels involves large, currently inexplicable conformational changes, these motions are qualitatively different in the two proteins, which may be a reflection of the dissimilar kinetics of closing.
The Journal of Membrane Biology – Springer Journals
Published: Jan 1, 2004
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