Physical mapping of herpes simplex virus type 1 ts mutants by marker rescue: Correlation of the physical and genetic maps

Parris, Deborah S.; Dixon, Richard A. F.; Schaffer, Priscilla A.

doi:10.1016/0042-6822(80)90519-x

Cited by 78 publications

(59 citation statements)

References 25 publications

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“…For brevity, in this paper the mutant is referred to as ts1207. The HSV-1 KOS mutants tsT36, tsV37 (Cb.u et al, 1979) and tsX45 (Machtiger et al, 1980), which have lesions within genome map units 0.49 to 0.64 (Parris et al, 1980;Pancake et al, 1983), were kindly provided by P. A. Schaffer.…”

Section: Methodsmentioning

confidence: 99%

Identification of a Herpes Simplex Virus Type 1 Polypeptide Which Is a Component of the Virus-induced Ribonucleotide Reductase

Preston

Palfreyman

Dutia

1984

Journal of General Virology

110

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Section: Methodsmentioning

confidence: 99%

Identification of a Herpes Simplex Virus Type 1 Polypeptide Which Is a Component of the Virus-induced Ribonucleotide Reductase

Preston

Palfreyman

Dutia

1984

Journal of General Virology

110

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“…Total DNA was purified from cultured cells using the DNeasy kit (Qiagen, Inc., Valencia, CA) according to the instructions of the manufacturer. In some cases as indicated, virions were purified from HSV-1 infected Vero cells by sedimentation through sucrose gradients and the DNA was extracted using phenol and chloroform as described previously [27,28]. DNA concentrations were determined using the Quant-IT DNA broad range assay kit (Molecular Probes, Inc., Eugene, OR) and adjusted to a final concentration of 100 g/ml.…”

Section: Ap Site Detectionmentioning

confidence: 99%

“…Cells harvested at 0 hr were not inoculated. For virion DNA preparations, Vero cells were inoculated with HSV-1 at low input multiplicity (0.1−0.5 plaque forming units/cell) and virions were purified from cells 72 hr later and DNA extracted as described previously [27,28]. Two independent virion preparations that had been stored at −80°C were tested.…”

mentioning

confidence: 99%

Mechanisms by which herpes simplex virus DNA polymerase limits translesion synthesis through abasic sites

et al. 2008

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Results suggest a high probability that abasic (AP) sites occur at least once per herpes simplex virus type 1 (HSV-1) genome. The parameters that control the ability of HSV-1 DNA polymerase (pol) to engage in AP translesion synthesis (TLS) were examined because AP lesions could influence the completion and fidelity of viral DNA synthesis. Pre-steady-state kinetic experiments demonstrated that wild-type (WT) and exonuclease-deficient (exo -) pol could incorporate opposite an AP lesion, but full TLS required absence of exo function. Virtually all of the WT pol was bound at the exo site to AP-containing P/Ts at equilibrium, and the pre-steady-state rate of excision by WT pol was higher on AP-containing than on matched DNA. However, several factors influencing polymerization work synergistically with exo activity to prevent HSV-1 pol from engaging in TLS. Although the pre-steady-state catalytic rate constant for insertion of dATP opposite a T or AP site was similar, ground-state binding affinity of dATP for insertion opposite an AP site was reduced 3−9-fold. Single-turnover running-start experiments demonstrated a reduced proportion of P/Ts extended to the AP site compared to the preceding site during processive synthesis by WT or exo -pol. Only the exo -pol engaged in TLS, though inefficiently and without burst kinetics, suggesting a much slower rate-limiting step for extension beyond the AP site.

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“…Virions were prepared from the extracellular medium and cytosol fraction of RK cells and were further fractionated on linear 20 to 60~ (w/w) sucrose gradients exactly as described previously (Parris et al, 1980). The virus band was collected and pelleted (35000g for 15 min).…”

Section: Cells and Virusesmentioning

confidence: 99%

“…Thymidine ([3H]TdR)-labelled and non-labelled SV40 supercoiled DNA (form I) were prepared as described previously (Trask et al, 1984). HSV DNA was prepared from purified virions as described by Parris et al (1980) and nick-translated by standard methods. Phage lambda DNA was obtained from commercial sources.…”

Section: Cells and Virusesmentioning

confidence: 99%

Association of Type I DNA Topoisomerase with Herpes Simplex Virus

Muller¹,

Bolles²,

Parris

1985

Journal of General Virology

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SUMMARYA topoisomerase activity is associated with herpes simplex virus type 1. The enzyme was recovered from purified virions which were disrupted with 6 M-guanidine HC1 followed by renaturation of extracted proteins. Based upon the following observations, the virion activity is classified as a type I topoisomerase: (i) the linking number of a unique DNA topoisomer is altered in steps of one; (ii) ATP and MgC12 are not required for activity; (iii) the enzyme can be trapped in a covalent complex with DNA; (iv) the covalent linkage to DNA is through a 3' phosphoryl bond. A number of lines of evidence strongly indicate that the topoisomerase is external to the nucleocapsid. For example, the activity was released by treatment of intact virions with NP40, and subsequent washing steps extracted most residual activity. When guanidine extracts were prepared from nucleocapsids, topoisomerase activity was not detectable. Finally, DNA within the virion did not appear to contain covalently attached proteins with properties similar to topoisomerases. Thus, the enzyme appears to be a component of the envelope or tegument structure of the virion.

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Physical mapping of herpes simplex virus type 1 ts mutants by marker rescue: Correlation of the physical and genetic maps

Cited by 78 publications

References 25 publications

Identification of a Herpes Simplex Virus Type 1 Polypeptide Which Is a Component of the Virus-induced Ribonucleotide Reductase

Identification of a Herpes Simplex Virus Type 1 Polypeptide Which Is a Component of the Virus-induced Ribonucleotide Reductase

Mechanisms by which herpes simplex virus DNA polymerase limits translesion synthesis through abasic sites

Association of Type I DNA Topoisomerase with Herpes Simplex Virus

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