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Journal of Bacteriology, May 1999, p. 2963-2965, Vol. 181, No. 9
0021-9193/99/$04.00+0

The C-Terminal Domain of DnaQ Contains the Polymerase Binding Site

Sharon A. Taft-Benz and Roel M. Schaaper*

Laboratory of Molecular Genetics, National Institute of Environmental Health Sciences, Research Triangle Park, North Carolina 27709

Received 22 September 1998/Accepted 22 February 1999

The Escherichia coli dnaQ gene encodes the 3'right-arrow5' exonucleolytic proofreading (varepsilon ) subunit of DNA polymerase III (Pol III). Genetic analysis of dnaQ mutants has suggested that varepsilon  might consist of two domains, an N-terminal domain containing the exonuclease and a C-terminal domain essential for binding the polymerase (alpha ) subunit. We have created truncated forms of dnaQ resulting in varepsilon  subunits that contain either the N-terminal or the C-terminal domain. Using the yeast two-hybrid system, we analyzed the interactions of the single-domain varepsilon  subunits with the alpha  and theta  subunits of the Pol III core. The DnaQ991 protein, consisting of the N-terminal 186 amino acids, was defective in binding to the alpha  subunit while retaining normal binding to the theta  subunit. In contrast, the NDelta 186 protein, consisting of the C-terminal 57 amino acids, exhibited normal binding to the alpha  subunit but was defective in binding to the theta  subunit. A strain carrying the dnaQ991 allele exhibited a strong, recessive mutator phenotype, as expected from a defective alpha  binding mutant. The data are consistent with the existence of two functional domains in varepsilon , with the C-terminal domain responsible for polymerase binding.

* Corresponding author. Mailing address: NIEHS, Laboratory of Molecular Genetics, MD E3-01, P.O. Box 12233, 111 T.W. Alexander Dr., Research Triangle Park, NC 27709. Phone: (919) 541-4043. Fax: (919) 541-7613. E-mail: schaaper{at}niehs.nih.gov.

Journal of Bacteriology, May 1999, p. 2963-2965, Vol. 181, No. 9
0021-9193/99/$04.00+0


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