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Nucleic Acids Research 2005 33(8):2504-2511; doi:10.1093/nar/gki549
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Published online 2 May 2005

© The Author 2005. Published by Oxford University Press. All rights reserved
The online version of this article has been published under an open access model. Users are entitled to use, reproduce, disseminate, or display the open access version of this article for non-commercial purposes provided that: the original authorship is properly and fully attributed; the Journal and Oxford University Press are attributed as the original place of publication with the correct citation details given; if an article is subsequently reproduced or disseminated not in its entirety but only in part or as a derivative work this must be clearly indicated. For commercial re-use, please contact journals.permissions{at}oupjournals.org

Article

Activity of Lac repressor anchored to the Escherichia coli inner membrane

Boris Görke, Jana Reinhardt and Bodo Rak*

Institut für Biologie III, Universität Freiburg Schänzlestrasse 1, D-79104 Freiburg, Germany

*To whom correspondence should be addressed. Tel: +49 761 203 2729; Fax: +49 761 203 2769; Email: bodo.rak{at}biologie.uni-freiburg.de

Received March 11, 2005. Revised April 15, 2005. Accepted April 15, 2005.

The transient inactivation of gene regulatory proteins by their sequestration to the cytoplasmic membrane in response to cognate signals is an increasingly recognized mechanism of gene regulation in bacteria. It remained to be shown, however, whether tethering to the membrane per se could be responsible for inactivation, i.e. whether such relocation leads to a spatial separation from the chromosome that results in inactivity or whether other mechanisms are involved. We, therefore, investigated the activity of Lac repressor artificially attached to the Escherichia coli cytoplasmic membrane. We demonstrate that this chimeric protein perfectly represses transcription initiated at the tac operator–promoter present on a plasmid and even in the chromosome. Moreover, this repression is inducible as normal. The data suggest that proteins localized to the inner face of the cytoplasmic membrane in principle have unrestricted access to the chromosome. Thus sequestration to the membrane in terms of physical separation from the chromosome cannot account alone for the inactivation of regulatory proteins. Other mechanisms, like induction of a conformational change or masking of binding domains are required additionally.

Present addresses: Boris Görke, Abteilung für Allgemeine Mikrobiologie, Institut für Mikrobiologie und Genetik, Georg-August-Universität Göttingen, Grisebachstrasse 8, D-37077 Göttingen, Germany

Jana Reinhardt, CellGenix Technologie Transfer GmbH, Am Fughafen 16, D-79108 Freiburg, Germany

The authors wish it to be known that, in their opinion, the first two authors should be regarded as joint First Authors


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