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Strand-specific loading of DnaB helicase by DnaA to a substrate mimicking unwound oriC

MPG-Autoren

Weigel,  Christoph
Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons50550

Seitz,  Harald
Dept. of Vertebrate Genomics (Head: Hans Lehrach), Max Planck Institute for Molecular Genetics, Max Planck Society;

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Zitation

Weigel, C., & Seitz, H. (2002). Strand-specific loading of DnaB helicase by DnaA to a substrate mimicking unwound oriC. Molecular Microbiology, 46(4), 1149-1156.


Zitierlink: http://hdl.handle.net/11858/00-001M-0000-0010-8B85-B
Zusammenfassung
We analysed the enzymatic activity (strand dis-placement) of the Escherichia coli DnaB helicase on a mirror-image pair of oligonucleotide-based substrates mimicking the unwound replication origin oriC. Loading of the helicase complex occurred exclusively to the single-stranded 'lower strand' part of the substrates. Full helicase activity required DnaA bound to the double-stranded part of the substrates (oriC DnaA box R1) and to their single-stranded 'upper strand' part. We assume that in vivo DnaA also loads the first of two helicase complexes - required for the assembly of two replication forks - to the lower strand of oriC during initiation of bidirectional chromosome replication in E. coli.