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Nucleic Acids Research, 2001, Vol. 29, No. 24 5107-5114
© 2001 Oxford University Press

An architectural role of the Escherichia coli chromatin protein FIS in organising DNA

Robert Schneider, Rudolf Lurz1, Gerhild Lüder1, Carolin Tolksdorf2, Andrew Travers3 and Georgi Muskhelishvili*

Institut fuer Genetik und Mikrobiologie, LMU Muenchen, Maria-Ward-Strasse 1a, D-80638 Muenchen, Germany, 1Max-Planck-Institut fuer Molekulare Genetik, Ihnestrasse 73, D-14195 Berlin, Germany, 2Sektion Physik, Lehrstuhl fuer angewandte Physik, LMU Muenchen, Amalienstrasse 54, D-80799 Muenchen, Germany and 3MRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 2QH, UK

The Escherichia coli chromatin protein FIS modulates the topology of DNA in a growth phase-dependent manner. In this study we have investigated the global effect of FIS binding on DNA architecture in vitro. We show that in supercoiled DNA molecules FIS binds at multiple sites in a non-random fashion and increases DNA branching. This global DNA reshaping effect is independent of the helical phasing of FIS binding sites. We propose, in addition to the previously inferred stabilisation of tightly bent DNA microloops in the upstream regions of certain promoters, that FIS may perform the distinct architectural function of organising branched plectonemes in the E.coli nucleoid.

* To whom correspondence should be addressed at present address: Max-Planck-Institut fuer terrestrische Mikrobiologie, Karl-von-Frisch-Strasse, D-35043 Marburg, Germany. Tel: +49 6421 178 600; Fax: +49 6421 178 609; Email: muskheli{at}mailer.uni-marburg.de


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