Nucleic Acids Research, 2000, Vol. 28, No. 2 552-559
© 2000 Oxford University Press
Bacillus subtilis LrpC is a sequence-independent DNA-binding and DNA-bending protein which bridges DNA
Departamento de Biotecnología Microbiana, Centro Nacional de Biotecnología, CSIC, Campus Universidad Autónoma de Madrid, Cantoblanco, 28049 Madrid, Spain
Genetic evidence suggests that the Bacillus subtilis lrpC gene product participates in cell growth and sporulation. The purified LrpC protein, which has a predicted molecular mass of 16.4 kDa, is a tetramer in solution. LrpC binds with higher affinity (Kapp ~ 80 nM) to intrinsically curved DNA than to non-curved DNA (Kapp ~ 700 nM). DNase I footprinting and the supercoiling of relaxed circular plasmid DNA in the presence of topoisomerase I revealed that LrpC induces DNA bending and constrains DNA supercoils in vitro. The LrpC protein cooperatively increases DNA binding of the bona fide DNA-binding and DNA-bending protein Hbsu. LrpC forms inter- and intramolecular bridges on linear and supercoiled DNA molecules, resulting in a large network and DNA compactation. Collectively, these findings suggest that LrpC is an architectural protein and that its activities could provide a means to modulate DNA transactions.
* To whom correspondence should be addressed. Tel: +34 91585 4528; Fax: +34 91585 4506; Email: sayora@cnb.uam.es Present address: Angels Tapias, Departamento de Genética y Microbiología, Universitat Autónoma de Barcelona, Bellaterra, 08193 Barcelona, Spain
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