Journal
MOLECULAR MICROBIOLOGY
Volume 46, Issue 4, Pages 1149-1156Publisher
BLACKWELL PUBLISHING LTD
DOI: 10.1046/j.1365-2958.2002.03232.x
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We analysed the enzymatic activity (strand displacement) 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.
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