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Protein Translocation by Bacterial Toxin Channels: A Comparison of Diphtheria Toxin and Colicin Ia

Zhengyan Wu ^*, Karen S. Jakes ^*, Ben S. Samelson-Jones ^*, Bing Lai , Gang Zhao , Erwin London  and Alan Finkelstein ^*

^* Department of Physiology and Biophysics, Albert Einstein College of Medicine, Bronx, New York 10461; and Department of Biochemistry and Cell Biology, State University of New York, Stony Brook, New York 11794

Correspondence: Address reprint requests to Karen S. Jakes, Albert Einstein College of Medicine, Dept. of Physiology and Biophysics, 1300 Morris Park Avenue, Bronx, NY 10461. Tel.: 718-430-3169; E-mail: jakes{at}aecom.yu.edu.

Regions of both colicin Ia and diphtheria toxin N-terminal to the channel-forming domains can be translocated across planar phospholipid bilayer membranes. In this article we show that the translocation pathway of diphtheria toxin allows much larger molecules to be translocated than does the translocation pathway of colicin Ia. In particular, the folded A chain of diphtheria toxin is readily translocated by that toxin but is not translocated by colicin Ia. This difference cannot be attributed to specific recognition of the A chain by diphtheria toxin's translocation pathway because the translocation pathway also accommodates folded myoglobin.

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