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, Alan Finkelstein

Research output: Contribution to journalArticle

8 Scopus citations

Abstract

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.

Original languageEnglish (US)
Pages (from-to)3249-3256
Number of pages8
JournalBiophysical journal
Volume91
Issue number9
DOIs
Publication statusPublished - Nov 2006

    Fingerprint

ASJC Scopus subject areas

  • Biophysics

Cite this

Wu, Z., Jakes, K. S., Samelson-Jones, B. S., Lai, B., Zhao, G., London, E., & Finkelstein, A. (2006). Protein translocation by bacterial toxin channels: A comparison of diphtheria toxin and colicin Ia. Biophysical journal, 91(9), 3249-3256. https://doi.org/10.1529/biophysj.106.085753