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Nucleic Acids Research 2004 32(19):5935-5944; doi:10.1093/nar/gkh915
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Published online 8 November 2004

Nucleic Acids Research, Vol. 32 No. 19 © Oxford University Press 2004; all rights reserved

DNA condensation and self-aggregation of Escherichia coli Dps are coupled phenomena related to the properties of the N-terminus

Pierpaolo Ceci, Sara Cellai1, Elisabetta Falvo, Claudio Rivetti1, Gian Luigi Rossi1 and Emilia Chiancone*

C.N.R. Institute of Molecular Biology and Pathology, Department of Biochemical Sciences ‘A. Rossi-Fanelli’, University of Rome ‘La Sapienza’, 00185 Rome, Italy and 1 Department of Biochemistry and Molecular Biology, University of Parma, 43100 Parma, Italy

* To whom correspondence should be addressed. Tel: +39 06 4940543; +39 06 49910761; Fax: +39 06 4440062; Email: emilia.chiancone{at}uniroma1.it

Received July 30, 2004; Revised September 17, 2004; Accepted October 11, 2004

Escherichia coli Dps (DNA-binding proteins from starved cells) is the prototype of a DNA-protecting protein family expressed by bacteria under nutritional and oxidative stress. The role of the lysine-rich and highly mobile Dps N-terminus in DNA protection has been investigated by comparing the self-aggregation and DNA-condensation capacity of wild-type Dps and two N-terminal deletion mutants, Dps{Delta}8 and Dps{Delta}18, lacking two or all three lysine residues, respectively. Gel mobility and atomic force microscopy imaging showed that at pH 6.3, both wild type and Dps{Delta}8 self-aggregate, leading to formation of oligomers of variable size, and condense DNA with formation of large Dps–DNA complexes. Conversely, Dps{Delta}18 does not self-aggregate and binds DNA without causing condensation. At pH 8.2, Dps{Delta}8 and Dps{Delta}18 neither self-aggregate nor cause DNA condensation, a behavior also displayed by wild-type Dps at pH 8.7. Thus, Dps self-aggregation and Dps-driven DNA condensation are parallel phenomena that reflect the properties of the N-terminus. DNA protection against the toxic action of Fe(II) and H2O2 is not affected by the N-terminal deletions either in vitro or in vivo, in accordance with the different structural basis of this property.


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