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Papers In Press, published online ahead of print August 2, 2002
J. Biol. Chem, 10.1074/jbc.M205031200
Submitted on May 22, 2002
Revised on July 31, 2002
Accepted on August 1, 2002

E. coli DnaA protein loads a single DnaB helicase at a DnaA box hairpin

Kevin M Carr and Jon M. Kaguni

Department of Biochemistry, Michigan State University, East Lansing, MI 48824-1319

Corresponding Author: kaguni{at}pilot.msu.edu

The molecular engine that drives bidirectional replication fork movement from the E. coli replication origin (oriC) is the replicative helicase, DnaB. At oriC, two and only two helicase molecules are loaded, one for each replication fork. DnaA participates in helicase loading; DnaC is also involved because it must be in a complex with DnaB for delivery of the helicase. As DnaA induces a local unwinding of oriC, one model is that the limited availability of single-stranded DNA at oriC restricts the number of DnaB molecules that can bind. In this report, we determined that one DnaB helicase or one DnaB-DnaC complex is bound to a single-stranded DNA in a biologically relevant DNA replication system. These results indicate that the availability of single-stranded DNA is not a limiting factor. Instead, the results support a model in which the site of entry for DnaB is altered so that it cannot be reused.


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