DNA polymerases of eukaryotes

Holmes, Andrew M.; Johnston, Irving R.

doi:10.1016/0014-5793(75)80721-6

Cited by 65 publications

(17 citation statements)

References 132 publications

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“…These activities were identified as DNA polymerases CI and y [19,20] respectively, on the basis of their response to inhibitors. Treatment with 1 m M N-ethylmaleimide resulted in 97'x inhibition of the 266-kDa activity and 85 "/, inhibition of the 72-kDa enzyme, characteristic of the CI and y DNA polymerases respectively [19,20]. The responses of the two peaks to 2',3'-deoxythymidine triphosphate were also characteristic of those described for DNA polymerases CI and y [21].…”

Section: Gel Filtration Oj a Salt Extract Of Hbp-all Cellsmentioning

confidence: 99%

“…(dT),o (data not shown). The apparent molecular mass of this peak (43 kDa) and its preference for a synthetic ribohomopolymer template suggested its identity as being DNA polymerase /I [19,20,22]. However, upon concentration and dialysis this peak was found to represent only 6 of the total recovered D N A polymerase and was not characterised further.…”

Section: Gel Filtration Oj a Salt Extract Of Hbp-all Cellsmentioning

confidence: 99%

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Solubilization and Partial Characterization of a Multienzyme Complex of DNA Synthesis from Human Lymphoblastoid Cells

Wickremasinghe

Yaxley

Hoffbrand

1982

European Journal of Biochemistry

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Gently lysed human lymphoblastoid cells (HPB-ALLDeoxynucleoside triphosphates are the immediate precursors for DNA synthesis in all cells [I]. In mammalian cells these precursors are synthesized either by salvage of preformed nucleosides or are derived from RNA precursors synthesized from small molecules (de novo pathway). In virusinfected bacteria the enzymes of DNA precursor synthesis form a multienzyme complex together with DNA polymerase [2,3]. This complex channels distal precursors efficiently into DNA and maintains a higher concentration of deoxynucleoside triphosphates at the site of replication than would be built up by freely diffusing enzymes. The maintenance of concentration gradients of metabolites by the activity of multienzyme complexes is referred to as functional compartmentation [4]. Deoxynucleoside triphosphates are also functionally compartmentalized in mammalian cells [5 -91. Chinese hamster embryo fibroblasts, permeabilized by lysolecithin treatment, incorporated ribonucleoside diphosphates into DNA in preference to deoxynucleoside triphosphates [lo]. These authors suggested that a multienzyme complex for channelling distal DNA precursors into DNA also operated in mammalian cells. In this communication we describe the solubilization of a DNA-synthetic multienzyme complex from HPB-ALL cells, a cultured human lymphoblastoid cell line. Experiments involving incorporation of distal precursors into DNA strongly suggest the existence of such a complex. The putative complex has also been isolated by gel filtration.

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Section: Gel Filtration Oj a Salt Extract Of Hbp-all Cellsmentioning

confidence: 99%

Section: Gel Filtration Oj a Salt Extract Of Hbp-all Cellsmentioning

confidence: 99%

Solubilization and Partial Characterization of a Multienzyme Complex of DNA Synthesis from Human Lymphoblastoid Cells

Wickremasinghe

Yaxley

Hoffbrand

1982

European Journal of Biochemistry

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“…It has been shown that the DNA polymerases of mammalian cells differ considerably from the DNA polymerases of micro-organisms, and several reviews on the properties of mammalian DNA polymerases have recently appeared [6][7][8][9][10][11]. The mammalian DNA ligases also differ in many respects from bacterial DNA ligases, but the properties of the DNA ligases of higher organisms have not been previously reviewed.…”

Section: Introductionmentioning

confidence: 99%

DNA ligases of eukaryotes

1976

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“…All cells so far studied have shown more than one enzyme with DNA polymerase properties (Holmes & Johnston, 1975;. Further, it has been demonstrated that enzymic activities can be associated with subcellular structures such as nuclei (Bernard et al, 1974), mitochondria (Meyer & Simpson, 1970) and cytoplasmic membrane fractions (Matsukage et al, 1974).…”

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confidence: 99%

The heterogeneity of cytoplasmic deoxyribonucleic acid polymerase from Physarum polycephalum

Zänker¹,

Schiebel²

1978

Biochemical Journal

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Cytoplasmic DNA polymerase (DNA deoxynucleotidyltransferase, EC 2.7.7.7) was partially purified from Physarum polycephalum. The first step ofthe purification procedure utilized the fact that the enzyme on gel filtration behaves in anomalous fashion. The second step was either ion-exchange chromatography or sucrose-density-gradient centrifugation. The partially purified DNA polymerase was heterogeneous and at least four species with different sedimentation coefficients (5.5 S, 7.2 S, 8.6 S and 11.5 S) were detected. Calculated molecular weights indicated a tendency for stoicheiometric polypeptide aggregation, accompanied by an alteration of the three-dimensional structure from a compact spheroid to a more open elliptical form. Sodium dodecyl sulphate/polyacrylamide-gel electrophoresis and computed molecular weights suggest an active protomer in the range of 113000 daltons; all data pertain to I 0.045, which was maintained during the whole procedure.

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DNA polymerases of eukaryotes

Cited by 65 publications

References 132 publications

Solubilization and Partial Characterization of a Multienzyme Complex of DNA Synthesis from Human Lymphoblastoid Cells

Solubilization and Partial Characterization of a Multienzyme Complex of DNA Synthesis from Human Lymphoblastoid Cells

DNA ligases of eukaryotes

The heterogeneity of cytoplasmic deoxyribonucleic acid polymerase from Physarum polycephalum

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