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The structure of bacterial DnaA: implications for general mechanisms underlying DNA replication initiation
Author(s) -
Erzberger Jan P.,
Pirruccello Michelle M.,
Berger James M.
Publication year - 2002
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1093/emboj/cdf496
Subject(s) - dnaa , biology , origin recognition complex , pre replication complex , seqa protein domain , aquifex aeolicus , dna replication , origin of replication , eukaryotic dna replication , dnab helicase , genetics , control of chromosome duplication , minichromosome maintenance , microbiology and biotechnology , helicase , dna , rna , gene , escherichia coli
The initiation of DNA replication is a key event in the cell cycle of all organisms. In bacteria, replication initiation occurs at specific origin sequences that are recognized and processed by an oligomeric complex of the initiator protein DnaA. We have determined the structure of the conserved core of the Aquifex aeolicus DnaA protein to 2.7 Å resolution. The protein comprises an AAA+ nucleotide‐binding fold linked through a long, helical connector to an all‐helical DNA‐binding domain. The structure serves as a template for understanding the physical consequences of a variety of DnaA mutations, and conserved motifs in the protein suggest how two critical aspects of origin processing, DNA binding and homo‐oligomerization, are mediated. The spatial arrangement of these motifs in DnaA is similar to that of the eukaryotic‐like archaeal replication initiation factor Cdc6/Orc1, demonstrating that mechanistic elements of origin processing may be conserved across bacterial, archaeal and eukaryotic domains of life.