In the Bacillus stearothermophilus DnaB-DnaG complex, the activities of the two proteins are modulated by distinct but overlapping networks of residues.
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Mechanism and evolution of DNA primasesThe crystal structure of the Thermus aquaticus DnaB helicase monomerStructure of hexameric DnaB helicase and its complex with a domain of DnaG primaseThe structure of a DnaB-family replicative helicase and its interactions with primaseHexameric ring structure of the N-terminal domain of Mycobacterium tuberculosis DnaB helicaseCrystal Structure and Mode of Helicase Binding of the C-Terminal Domain of Primase from Helicobacter pyloriStructure of a helicase–helicase loader complex reveals insights into the mechanism of bacterial primosome assemblyPrimase is required for helicase activity and helicase alters the specificity of primase in the enteropathogen Clostridium difficileAllosteric regulation of the primase (DnaG) activity by the clamp-loader (tau) in vitro.Structural Insight into the Specific DNA Template Binding to DnaG primase in Bacteria.Two distantly homologous DnaG primases from Thermoanaerobacter tengcongensis exhibit distinct initiation specificities and priming activitiesZinc-binding domain of the bacteriophage T7 DNA primase modulates binding to the DNA template.Domain swapping reveals that the C- and N-terminal domains of DnaG and DnaB, respectively, are functional homologues.An in trans interaction at the interface of the helicase and primase domains of the hexameric gene 4 protein of bacteriophage T7 modulates their activities.Recent Advances in Helicobacter pylori Replication: Possible Implications in Adaptation to a Pathogenic Lifestyle and Perspectives for Drug Design.Functional interplay of DnaE polymerase, DnaG primase and DnaC helicase within a ternary complex, and primase to polymerase hand-off during lagging strand DNA replication in Bacillus subtilis.Class-specific restrictions define primase interactions with DNA template and replicative helicase.Staphylococcus aureus helicase but not Escherichia coli helicase stimulates S. aureus primase activity and maintains initiation specificity.Conserved residues of the C-terminal p16 domain of primase are involved in modulating the activity of the bacterial primosome.Hyperthermophilic Aquifex aeolicus initiates primer synthesis on a limited set of trinucleotides comprised of cytosines and guaninesDnaG Primase-A Target for the Development of Novel Antibacterial Agents
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P2860
In the Bacillus stearothermophilus DnaB-DnaG complex, the activities of the two proteins are modulated by distinct but overlapping networks of residues.
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In the Bacillus stearothermoph ...... rlapping networks of residues.
@en
In the Bacillus stearothermoph ...... rlapping networks of residues.
@nl
type
label
In the Bacillus stearothermoph ...... rlapping networks of residues.
@en
In the Bacillus stearothermoph ...... rlapping networks of residues.
@nl
prefLabel
In the Bacillus stearothermoph ...... rlapping networks of residues.
@en
In the Bacillus stearothermoph ...... rlapping networks of residues.
@nl
P2860
P1476
In the Bacillus stearothermoph ...... rlapping networks of residues.
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P2093
Jenny Thirlway
P2860
P304
P356
10.1128/JB.188.4.1534-1539.2006
P407
P577
2006-02-01T00:00:00Z