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Papers In Press, published online ahead of print November 14, 2000
J. Biol. Chem, 10.1074/jbc.M009827200
Submitted on October 27, 2000
Revised on November 14, 2000
Accepted on November 13, 2000

t binds and organizes Escherichia coli replication proteins through distinct Domain: Domain III, shared by gamma and t binds delta delta2 and cy

Dexiang Gao and Charles S. McHenry

Department of Biochemistry and Molecular Genetics, University of Colorado Health Sciences Center, Denver, CO 80262

Corresponding Author: charles.mchenry{at}uchsc.edu

The DnaX complex of the DNA polymerase holoenzyme assembles the b2 processivity factor onto the primed template enabling highly processive replication. The key ATPases within this complex are t and g, alternative frameshift products of the dnaX gene. Of the five domains of t, I-III are shared with g (Gao, D. and McHenry, C. S. (2000) J Biol Chem 275 xxx-xxx). In vivo, g binds the auxiliary subunits dd¢ and cy (Glover, B. P. and McHenry, C. S. (2000) J Biol Chem 275, 3017-3020). To localize dd¢ and cy binding domains within g domains I-III, we measured the binding of purified biotin- tagged DnaX proteins lacking specific domains to dd¢ and cy by surface plasmon resonance. Fusion proteins containing either DnaX domains I-III or domains III-V bound dd¢ and cy subunits. A DnaX protein only containing domains I and II did not bind dd¢ or cy. The binding affinity of cy for DnaX domains I-III and domains III-V was the same as that of cy for full-length t, indicating that domain III contained all structural elements required for cy binding. Domain III of t also contained dd¢ binding sites, although the interaction between dd¢ and domains III-V of t was 10-fold weaker than the interaction between dd¢ and full length t. The presence of both d and cy strengthened the d¢-C(0)t interaction by at least 15-fold. Domain III was the only domain common to all of t fusion proteins whose interaction with d¢ was enhanced in the presence of d and cy. Thus, domain III of the DnaX proteins not only contains the dd¢ and cy binding sites, but also contains the elements required for the positive cooperative assembly of the DnaX complex.


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