Abstract:
:Loading of the replicative ring helicase onto the origin of replication (oriC) is the final outcome of a well coordinated series of events that collectively constitute a primosomal cascade. Once the ring helicase is loaded, it recruits the primase and signals the switch to the polymerization mode. The transient nature of the helicase-primase (DnaB-DnaG) interaction in the Escherichia coli system has hindered our efforts to elucidate its structure and function. Taking advantage of the stable DnaB-DnaG complex in Bacillus stearothermophilus, we have reviewed conflicting mutagenic data from other bacterial systems and shown that DnaG interacts with the flexible linker that connects the N- and C-terminal domains of DnaB. Furthermore, atomic force microscopy (AFM) imaging experiments show that binding of the primase to the helicase induces predominantly a 3-fold symmetric morphology to the hexameric ring. Overall, three DnaG molecules appear to interact with the hexameric ring helicase but a small number of complexes with two and even one DnaG molecule bound to DnaB were also detected. The structural/functional significance of these data is discussed and a speculative structural model for this complex is suggested.
journal_name
Nucleic Acids Resjournal_title
Nucleic acids researchauthors
Thirlway J,Turner IJ,Gibson CT,Gardiner L,Brady K,Allen S,Roberts CJ,Soultanas Pdoi
10.1093/nar/gkh628keywords:
subject
Has Abstractpub_date
2004-06-01 00:00:00pages
2977-86issue
10eissn
0305-1048issn
1362-4962pii
32/10/2977journal_volume
32pub_type
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