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. (Q33883880)

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English	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.	scientific article

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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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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

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13 January 2020

Stacy D Carrington-Lawrence

2

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Ping Bai

3

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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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14

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13 January 2020

9088-9096

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describes a project that uses

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

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

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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.

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

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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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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

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

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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.

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

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One more conserved sequence motif in helicases

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Identifiers

10.1128/JVI.79.14.9088-9096.2005

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13 January 2020

PMC publication ID

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13 January 2020

PubMed publication ID

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13 January 2020

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