Helicobacter pylori DnaB helicase can bypass Escherichia coli DnaC function in vivo
AUTOR(ES)
Soni, Rajesh K.
FONTE
Portland Press Ltd.
RESUMO
In Escherichia coli, DnaC is essential for loading DnaB helicase at oriC (the origin of chromosomal DNA replication). The question arises as to whether this model can be generalized to other species, since many eubacterial species fail to possess dnaC in their genomes. Previously, we have reported the characterization of HpDnaB (Helicobacter pylori DnaB) both in vitro and in vivo. Interestingly, H. pylori does not have a DnaC homologue. Using two different E. coli dnaC (EcdnaC) temperature-sensitive mutant strains, we report here the complementation of EcDnaC function by HpDnaB in vivo. These observations strongly suggest that HpDnaB can bypass EcDnaC activity in vivo.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=1175132Documentos Relacionados
- Functional characterization of Helicobacter pylori DnaB helicase
- The dnaC protein of Escherichia coli. Purification, physical properties and interaction with dnaB protein.
- Replication of bacteriophage phiK duplex replicative-form DNA in dnaB and dnaC mutants of Escherichia coli.
- Cryptic single-stranded-DNA binding activities of the phage λ P and Escherichia coli DnaC replication initiation proteins facilitate the transfer of E. coli DnaB helicase onto DNA
- Illegitimate Recombination Induced by Overproduction of DnaB Helicase in Escherichia coli