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Biophys. J. BioFAST: First Published August 11, 2006. doi:10.1529/biophysj.106.085753
© 2006 by the Biophysical Society.

A more recent version of this article appeared on November 1, 2006.
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Karen S. Jakes
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CHANNELS, RECEPTORS, AND ELECTRICAL SIGNALING

PROTEIN TRANSLOCATION BY BACTERIAL TOXIN CHANNELS: A COMPARISON OF DIPHTHERIA TOXIN AND COLICIN Ia

Zhengyan Wu 1, Karen S. Jakes 1*, Ben S. Samelson-Jones 1, Bing Lai 2, Gang Zhao 2, Erwin London 2 and Alan Finkelstein 1

1 Albert Einstein College of Medicine
2 State University of NY, Stony Brook

* To whom correspondence should be addressed. E-mail: jakes{at}aecom.yu.edu.

Submitted on March 27, 2006
Revised on May 3, 2006
Accepted on 1 August 2006


  Abstract
For both colicin Ia and diphtheria toxin, regions of these proteins N-terminal to the channel-forming domains can be translocated across planar phospholipid bilayer membranes. In this paper 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, since the translocation pathway also accommodates folded myoglobin.

Key Words: Membrane bilayers, protein folding




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M. S. Kent, H. Yim, J. K. Murton, S. Satija, J. Majewski, and I. Kuzmenko
Oligomerization of Membrane-Bound Diphtheria Toxin (CRM197) Facilitates a Transition to the Open Form and Deep Insertion
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[Abstract] [Full Text] [PDF]


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Copyright © 2006 by the Biophysical Society.