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http://purl.uniprot.org/citations/14871889http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/14871889http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/14871889http://www.w3.org/2000/01/rdf-schema#comment"Semi-conservative DNA synthesis reactions catalyzed by the bacteriophage T4 DNA polymerase holoenzyme are initiated by a strand displacement mechanism requiring gp32, the T4 single-stranded DNA (ssDNA)-binding protein, to sequester the displaced strand. After initiation, DNA helicase acquisition by the nascent replication fork leads to a dramatic increase in the rate and processivity of leading strand DNA synthesis. In vitro studies have established that either of two T4-encoded DNA helicases, gp41 or dda, is capable of stimulating strand displacement synthesis. The acquisition of either helicase by the nascent replication fork is modulated by other protein components of the fork including gp32 and, in the case of the gp41 helicase, its mediator/loading protein gp59. Here, we examine the relationships between gp32 and the gp41/gp59 and dda helicase systems, respectively, during T4 replication using altered forms of gp32 defective in either protein-protein or protein-ssDNA interactions. We show that optimal stimulation of DNA synthesis by gp41/gp59 helicase requires gp32-gp59 interactions and is strongly dependent on the stability of ssDNA binding by gp32. Fluorescence assays demonstrate that gp59 binds stoichiometrically to forked DNA molecules; however, gp59-forked DNA complexes are destabilized via protein-protein interactions with the C-terminal "A-domain" fragment of gp32. These and previously published results suggest a model in which a mobile gp59-gp32 cluster bound to lagging strand ssDNA is the target for gp41 helicase assembly. In contrast, stimulation of DNA synthesis by dda helicase requires direct gp32-dda protein-protein interactions and is relatively unaffected by mutations in gp32 that destabilize its ssDNA binding activity. The latter data support a model in which protein-protein interactions with gp32 maintain dda in a proper active state for translocation at the replication fork. The relationship between dda and gp32 proteins in T4 replication appears similar to the relationship observed between the UL9 helicase and ICP8 ssDNA-binding protein in herpesvirus replication."xsd:string
http://purl.uniprot.org/citations/14871889http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m311738200"xsd:string
http://purl.uniprot.org/citations/14871889http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m311738200"xsd:string
http://purl.uniprot.org/citations/14871889http://purl.uniprot.org/core/author"Ma Y."xsd:string
http://purl.uniprot.org/citations/14871889http://purl.uniprot.org/core/author"Ma Y."xsd:string
http://purl.uniprot.org/citations/14871889http://purl.uniprot.org/core/author"Wang T."xsd:string
http://purl.uniprot.org/citations/14871889http://purl.uniprot.org/core/author"Wang T."xsd:string
http://purl.uniprot.org/citations/14871889http://purl.uniprot.org/core/author"Giedroc D.P."xsd:string
http://purl.uniprot.org/citations/14871889http://purl.uniprot.org/core/author"Giedroc D.P."xsd:string
http://purl.uniprot.org/citations/14871889http://purl.uniprot.org/core/author"Morrical S.W."xsd:string
http://purl.uniprot.org/citations/14871889http://purl.uniprot.org/core/author"Morrical S.W."xsd:string
http://purl.uniprot.org/citations/14871889http://purl.uniprot.org/core/author"Villemain J.L."xsd:string
http://purl.uniprot.org/citations/14871889http://purl.uniprot.org/core/author"Villemain J.L."xsd:string
http://purl.uniprot.org/citations/14871889http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/14871889http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/14871889http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/14871889http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/14871889http://purl.uniprot.org/core/pages"19035-19045"xsd:string
http://purl.uniprot.org/citations/14871889http://purl.uniprot.org/core/pages"19035-19045"xsd:string
http://purl.uniprot.org/citations/14871889http://purl.uniprot.org/core/title"Dual functions of single-stranded DNA-binding protein in helicase loading at the bacteriophage T4 DNA replication fork."xsd:string
http://purl.uniprot.org/citations/14871889http://purl.uniprot.org/core/title"Dual functions of single-stranded DNA-binding protein in helicase loading at the bacteriophage T4 DNA replication fork."xsd:string
http://purl.uniprot.org/citations/14871889http://purl.uniprot.org/core/volume"279"xsd:string
http://purl.uniprot.org/citations/14871889http://purl.uniprot.org/core/volume"279"xsd:string
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