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Journal of Biochemistry Advance Access originally published online on July 7, 2006
Journal of Biochemistry 2006 140(2):275-283; doi:10.1093/jb/mvj147
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© 2006 The Japanese Biochemical Society.

Regular Paper

Characterization of Pores Formed by YaeT (Omp85) from Escherichia coli

Johannes F. Stegmeier and Christian Andersen*

Universität Würzburg, Lehrstuhl für Biotechnologie, Biozentrum der Universität Würzburg, Am Hubland, D-97074 Würzburg, Germany

* To whom correspondence should be addressed. Phone: +49-931-888-4510, Fax: +49-931-888-4509, E-mail: andersen{at}biozentrum.uni-wuerzburg.de

Proteins of the Omp85 family play a major role in the biogenesis of the bacterial outer membrane, since they were shown to mediate insertion of outer membrane proteins. The Escherichia coli Omp85 homologue YaeT is essential for viability, but its exact mode of action is not yet elucidated. We could show that YaeT is composed of two distinct domains, an amino-terminal periplasmic and a carboxy-terminal membrane domain. The full length YaeT and the isolated membrane domain induce pores when reconstituted in planar lipid membranes. The pores exhibit a certain variability of conductance indicating a flexible structure, which could be an essential property of a lateral opening channel releasing proteins into the bacterial outer membrane. We could further show that the periplasmic domain proves to be essential for in vivo function of YaeT.


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