Dnab helicase is recruited to the replication initiation complex via binding of dnaa domain i to the lateral surface of the dnab n-terminal domain

HIGHLIGHTS

  • who: Chihiro Hayashi from the Departments of Molecular Biology and Protein Structure, Function, and Design, Kyushu University Graduate School of and Welfare, Okawa, Japan have published the research work: DnaB helicase is recruited to the replication initiation complex via binding of DnaA domain I to the lateral surface of the DnaB N-terminal domain, in the Journal: (JOURNAL)
  • what: The authors showed that DnaB Leu160 in the C-terminal helix of the NTD is essential in DnaA binding. The authors propose that the DnaB Leu160- mediated interaction with DnaA plays a predominant role in the . . .

     

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