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J. Biol. Chem., Vol. 278, Issue 30, 28284-28293, July 25, 2003

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Characterization of the DNA Damage-inducible Helicase DinG from Escherichia coli^*

Oleg N. Voloshin, Filip Vanevski, Pavel P. Khil and R. Daniel Camerini-Otero 

From the Genetics and Biochemistry Branch, NIDDK, National Institutes of Health, Bethesda, Maryland 20892

The dinG promoter was first isolated in a genetic screen scoring for damage-inducible loci in Escherichia coli (Lewis, L. K., Jenkins, M. E., and Mount, D. W. (1992) J. Bacteriol. 174, 3377–3385). Sequence analysis suggests that the dinG gene encodes a putative helicase related to a group of eukaryotic helicases that includes mammalian XPD (Koonin, E. V. (1993) Nucleic Acids Res. 21, 1497), an enzyme involved in transcription-coupled nucleotide excision repair and basal transcription. We have characterized the dinG gene product from E. coli using genetic and biochemical approaches. Deletion of dinG has no severe phenotype, indicating that it is non-essential for cell viability. Both dinG deletion and over-expression of the DinG protein from a multicopy plasmid result in a slight reduction of UV resistance. DinG, purified as a fusion protein from E. coli cells, behaves as a monomer in solution, as judged from gel filtration experiments. DinG is an ATP-hydrolyzing enzyme; single-stranded (ss) DNA stimulates the ATPase activity 15-fold. Kinetic data yield a Hill coefficient of 1, consistent with one ATP-hydrolyzing site per DinG molecule. DinG possesses a DNA helicase activity; it translocates along ssDNA in a 5' 3' direction, as revealed in experiments with substrates containing non-natural 5'–5' and 3'–3' linkages. The ATP-dependent DNA helicase activity of DinG requires divalent cations (Mg²⁺, Ca²⁺, and Mn²⁺) but is not observed in the presence of Zn²⁺. The DinG helicase does not discriminate between ribonucleotide and deoxyribonucleotide triphosphates, and it unwinds duplex DNA with similar efficiency in the presence of ATP or dATP. We discuss the possible involvement of the DinG helicase in DNA replication and repair processes.

Received for publication, February 4, 2003 , and in revised form, April 21, 2003.

^* The costs of publication of this article were defrayed in part by the payment of page charges. This 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: Bldg. 5, Rm. 205A, 5 Memorial Dr. MSC 0538, Bethesda, MD 20892-0538. Tel.: 301-496-2710; Fax: 301-496-9878; E-mail: camerini{at}ncifcrf.gov.

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