(Q33883880)

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Mutations in the putative zinc-binding motif of UL52 demonstrate a complex interdependence between the UL5 and UL52 subunits of the human herpes simplex virus type 1 helicase/primase complex.

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13 January 2020

Mutations in the putative zinc-binding motif of UL52 demonstrate a complex interdependence between the UL5 and UL52 subunits of the human herpes simplex virus type 1 helicase/primase complex (English)

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:15994803%20AND%20SRC:MED&resulttype=core&format=json

13 January 2020

Herpes simplex virus type 1

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inferred from title

Sandra K. Weller

4

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13 January 2020

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Yan Chen

1

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13 January 2020

Stacy D Carrington-Lawrence

2

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13 January 2020

Ping Bai

3

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13 January 2020

publication date

1 July 2005

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13 January 2020

Journal of Virology

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13 January 2020

79

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13 January 2020

14

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13 January 2020

9088-9096

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13 January 2020

describes a project that uses

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11 June 2022

https://www.ebi.ac.uk/europepmc/webservices/rest/PMC1168741/fullTextXML

based on heuristic

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Crystal structure of RecBCD enzyme reveals a machine for processing DNA breaks

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Zinc fingers--folds for many occasions

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Recruitment of polymerase to herpes simplex virus type 1 replication foci in cells expressing mutant primase (UL52) proteins.

1 reference

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The UL5 and UL52 subunits of the herpes simplex virus type 1 helicase-primase subcomplex exhibit a complex interdependence for DNA binding.

1 reference

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Leading and lagging strand DNA synthesis in vitro by a reconstituted herpes simplex virus type 1 replisome

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The Cys4 zinc finger of bacteriophage T7 primase in sequence-specific single-stranded DNA recognition.

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A mutation in the C-terminal putative Zn2+ finger motif of UL52 severely affects the biochemical activities of the HSV-1 helicase-primase subcomplex.

1 reference

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In vitro processing of herpes simplex virus type 1 DNA replication intermediates by the viral alkaline nuclease, UL12

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Herpes simplex virus type-1 single-strand DNA-binding protein (ICP8) enhances the ability of the viral DNA helicase-primase to unwind cisplatin-modified DNA.

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An intertypic herpes simplex virus helicase-primase complex associated with a defect in neurovirulence has reduced primase activity.

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The UL8 subunit of the heterotrimeric herpes simplex virus type 1 helicase-primase is required for the unwinding of single strand DNA-binding protein (ICP8)-coated DNA substrates

1 reference

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Herpes simplex virus DNA replication

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A functional interaction of ICP8, the herpes simplex virus single-stranded DNA-binding protein, and the helicase-primase complex that is dependent on the presence of the UL8 subunit

1 reference

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5 July 2018

Biochemical analyses of mutations in the HSV-1 helicase-primase that alter ATP hydrolysis, DNA unwinding, and coupling between hydrolysis and unwinding

1 reference

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Mechanisms of helicase-catalyzed DNA unwinding

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The herpes simplex virus type 1 UL8 protein influences the intracellular localization of the UL52 but not the ICP8 or POL replication proteins in virus-infected cells

1 reference

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The UL8 subunit of the herpes simplex virus type-1 DNA helicase-primase optimizes utilization of DNA templates covered by the homologous single-strand DNA-binding protein ICP8.

1 reference

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The role of the zinc motif in sequence recognition by DNA primases

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Replacement of gly815 in helicase motif V alters the single-stranded DNA-dependent ATPase activity of the herpes simplex virus type 1 helicase-primase

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Novel zinc finger motif in the basal transcriptional machinery: three-dimensional NMR studies of the nucleic acid binding domain of transcriptional elongation factor TFIIS

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Helicase-primase complex of herpes simplex virus type 1: a mutation in the UL52 subunit abolishes primase activity.

1 reference

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Requirement for a zinc motif for template recognition by the bacteriophage T7 primase

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The herpes simplex virus type 1 origin-binding protein interacts specifically with the viral UL8 protein

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The Aspergillus PacC zinc finger transcription factor mediates regulation of both acid- and alkaline-expressed genes by ambient pH.

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One more conserved sequence motif in helicases

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Overexpression and assembly of the herpes simplex virus type 1 helicase-primase in insect cells

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Association of DNA helicase and primase activities with a subassembly of the herpes simplex virus 1 helicase-primase composed of the UL5 and UL52 gene products

1 reference

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The UL8 subunit of the herpes simplex virus helicase-primase complex is required for efficient primer utilization

1 reference

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On the cellular localization of the components of the herpes simplex virus type 1 helicase-primase complex and the viral origin-binding protein

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Mechanism of primer synthesis by the herpes simplex virus 1 helicase-primase

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Key role of template sequence for primer synthesis by the herpes simplex virus 1 helicase-primase

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The role of zinc and the reactivity of cysteines in Escherichia coli primase

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The UL8 component of the herpes simplex virus helicase-primase complex stimulates primer synthesis by a subassembly of the UL5 and UL52 components.

1 reference

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Identifiers

10.1128/JVI.79.14.9088-9096.2005

1 reference

Europe PubMed Central

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:15994803%20AND%20SRC:MED&resulttype=core&format=json

13 January 2020

PMC publication ID

1 reference

Europe PubMed Central

PMC publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:15994803%20AND%20SRC:MED&resulttype=core&format=json

13 January 2020

PubMed publication ID

1 reference

Europe PubMed Central

PMC publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:15994803%20AND%20SRC:MED&resulttype=core&format=json

13 January 2020

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