An architectural role of the Escherichia coli chromatin protein FIS in organising DNA.
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.
Schneider
R
R
Institut fuer Genetik und Mikrobiologie, LMU Muenchen, Maria-Ward-Strasse 1a, D-80638 Muenchen, Germany.
Lurz
R
R
Lüder
G
G
Tolksdorf
C
C
Travers
A
A
Muskhelishvili
G
G
D002352:Carrier Proteins / Q000378:metabolism* / Q000502:physiology; D004269:DNA, Bacterial / Q000737:chemistry* / Q000378:metabolism / Q000648:ultrastructure; D004278:DNA, Superhelical / Q000737:chemistry / Q000378:metabolism / Q000648:ultrastructure; D004926:Escherichia coli / Q000737:chemistry / Q000235:genetics*; D029968:Escherichia coli Proteins; D035021:Factor For Inversion Stimulation Protein; D034982:Integration Host Factors; D018625:Microscopy, Atomic Force; D008854:Microscopy, Electron; D009690:Nucleic Acid Conformation; D010957:Plasmids / Q000737:chemistry / Q000378:metabolism / Q000648:ultrastructure; D011485:Protein Binding
D002352:Carrier Proteins; D004269:DNA, Bacterial; D004278:DNA, Superhelical; D029968:Escherichia coli Proteins; D035021:Factor For Inversion Stimulation Protein; D034982:Integration Host Factors; C440502:integration host factor, E coli