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J. Biol. Chem., Vol. 277, Issue 3, 2146-2150, January 18, 2002
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From the The Escherichia coli H-NS protein is
a nucleoid-associated protein involved in both transcription regulation
and DNA compaction. Each of these processes involves H-NS-mediated
bridge formation between adjacent DNA helices. With respect to
transcription regulation, preferential binding sites in the promoter
regions of different genes have been reported, and generally these
regions are curved. Often H-NS binding sites overlap with promoter core
regions or with binding sites of other regulatory factors. Not in all
cases, however, transcriptional repression is the result of
preferential binding by H-NS to promoter regions leading to occlusion
of the RNA polymerase. In the case of the rrnB
P1, H-NS actually stimulates open complex formation by
forming a ternary RNAP·H-NS·DNA complex, while
simultaneously stabilizing it to such an extent that promoter clearance
cannot occur. To define the mechanism by which H-NS interferes at this
step in the initiation pathway, the architecture of the
RNAP·H-NS·DNA complex was analyzed by scanning force microscopy (SFM). The SFM images show that the DNA flanking the RNA polymerase in
open initiation complexes is bridged by H-NS. On the basis of these
data, we present a model for the specific repression of transcription
initation at the rrnB P1 by H-NS.
Structural Basis for H-NS-mediated Trapping of RNA Polymerase in
the Open Initiation Complex at the rrnB P1*
,
Laboratory of Molecular Genetics, Gorlaeus
Laboratories, Leiden Institute of Chemistry, Leiden University, P. O. Box 9502, 2300 RA Leiden, The Netherlands, the § Department
of Cell Biology and Genetics, Erasmus University, P. O. Box 1738, 3000 DR Rotterdam, The Netherlands, and the ¶ Institut für
Physikalische Biologie, Heinrich-Heine-Universität
Düsseldorf, Universitätsstrasse 1, D-40225
Düsseldorf, Germany
*
This work was supported by the Chemical Council of the
Netherlands Organization for Scientific Research (NWO-CW) and the
Deutsche Forschungsgemeinsschaft.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed: Laboratory of
Molecular Genetics, Gorlaeus Laboratories, Leiden Inst. of Chemistry, Leiden University, P. O. Box 9502, 2300 RA Leiden, The
Netherlands. Tel.: 31-71-5274773; Fax: 31-71-5274537; E-mail:
N.Goosen@chem.Leidenuniv.nl.
Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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