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Literature DB >> 8676514

Evidence that the nuclease activities associated with the herpes simplex type 1 DNA polymerase are due to the 3'-5' exonuclease.

Abstract

We investigated nuclease activities associated with the catalytic subunit of herpes simplex virus type 1 DNA polymerase. We confirm that a 3'-5' exonuclease copurifies with this enzyme. Previous reports suggested that a 5' DNase was intrinsic to the polymerase. Our preparation lacks such activity.

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Year: 1996 PMID： 8676514 PMCID： PMC190424

Source DB: PubMed Journal: J Virol ISSN： 0022-538X Impact factor: 5.103

9 in total

1. A general structure for DNA-dependent DNA polymerases.

Authors: L Blanco; A Bernad; M A Blasco; M Salas
Journal: Gene Date: 1991-04 Impact factor: 3.688

2. Mutations within conserved motifs in the 3'-5' exonuclease domain of herpes simplex virus DNA polymerase.

Authors: J D Hall; K L Orth; K L Sander; B M Swihart; R A Senese
Journal: J Gen Virol Date: 1995-12 Impact factor: 3.891

3. The herpes simplex virus type 1 UL42 gene product: a subunit of DNA polymerase that functions to increase processivity.

Authors: J Gottlieb; A I Marcy; D M Coen; M D Challberg
Journal: J Virol Date: 1990-12 Impact factor: 5.103

4. Enzymatic activities of overexpressed herpes simplex virus DNA polymerase purified from recombinant baculovirus-infected insect cells.

Authors: A I Marcy; P D Olivo; M D Challberg; D M Coen
Journal: Nucleic Acids Res Date: 1990-03-11 Impact factor: 16.971

3 in total

1. Herpes Simplex Virus 1 DNA Polymerase RNase H Activity Acts in a 3'-to-5' Direction and Is Dependent on the 3'-to-5' Exonuclease Active Site.

Authors: Jessica L Lawler; Purba Mukherjee; Donald M Coen
Journal: J Virol Date: 2018-02-12 Impact factor: 5.103

2. Evolution of viral DNA-dependent DNA polymerases.

Authors: C W Knopf
Journal: Virus Genes Date: 1998 Impact factor: 2.198

3. Herpes simplex virus processivity factor UL42 imparts increased DNA-binding specificity to the viral DNA polymerase and decreased dissociation from primer-template without reducing the elongation rate.

Authors: K Weisshart; C S Chow; D M Coen
Journal: J Virol Date: 1999-01 Impact factor: 5.103

3 in total

Evidence that the nuclease activities associated with the herpes simplex type 1 DNA polymerase are due to the 3'-5' exonuclease.

1. A general structure for DNA-dependent DNA polymerases.

2. Mutations within conserved motifs in the 3'-5' exonuclease domain of herpes simplex virus DNA polymerase.

3. The herpes simplex virus type 1 UL42 gene product: a subunit of DNA polymerase that functions to increase processivity.

4. Enzymatic activities of overexpressed herpes simplex virus DNA polymerase purified from recombinant baculovirus-infected insect cells.

5. Herpes simplex-1 DNA polymerase. Identification of an intrinsic 5'----3' exonuclease with ribonuclease H activity.

6. The herpes simplex virus type I DNA polymerase. Polypeptide structure and antigenic domains.

7. Structural and functional organization of herpes simplex virus DNA polymerase investigated by limited proteolysis.

8. Comparison of exonucleolytic activities of herpes simplex virus type-1 DNA polymerase and DNase.

9. Properties of herpes simplex virus DNA polymerase and characterization of its associated exonuclease activity.

1. Herpes Simplex Virus 1 DNA Polymerase RNase H Activity Acts in a 3'-to-5' Direction and Is Dependent on the 3'-to-5' Exonuclease Active Site.

2. Evolution of viral DNA-dependent DNA polymerases.

3. Herpes simplex virus processivity factor UL42 imparts increased DNA-binding specificity to the viral DNA polymerase and decreased dissociation from primer-template without reducing the elongation rate.