Literature DB >> 1319931

The effect of the UL42 protein on the DNA polymerase activity of the catalytic subunit of the DNA polymerase encoded by herpes simplex virus type 1.

G J Hart1, R E Boehme.   

Abstract

The effect that the UL42 protein of herpes simplex virus type 1 has on the DNA polymerase activity of the DNA polymerase catalytic subunit (Pol) of the same virus has been investigated. The observed effects are critically dependent on the salt used and its concentration, such that the UL42 protein may inhibit, have little or no effect on, or activate the Pol activity, depending on the condition used. The observed effects are due to the values for Km(app) for activated DNA and Vmaxapp for Pol and the Pol-UL42 protein complex differently varying with salt concentration.

Entities:  

Mesh：

Substances：

Year:  1992        PMID： 1319931     DOI： 10.1016/0014-5793(92)80872-e

Source DB:  PubMed          Journal:  FEBS Lett        ISSN： 0014-5793            Impact factor:   4.124


  8 in total

1.  Evidence against a simple tethering model for enhancement of herpes simplex virus DNA polymerase processivity by accessory protein UL42.

Authors:  Murari Chaudhuri; Deborah S Parris
Journal:  J Virol       Date:  2002-10       Impact factor: 5.103

2.  Effects of substitutions of arginine residues on the basic surface of herpes simplex virus UL42 support a role for DNA binding in processive DNA synthesis.

Authors:  John C W Randell; Gloria Komazin; Changying Jiang; Charles B C Hwang; Donald M Coen
Journal:  J Virol       Date:  2005-09       Impact factor: 5.103

3.  Cloning, expression, and functional characterization of the equine herpesvirus 1 DNA polymerase and its accessory subunit.

Authors:  Arianna Loregian; Alessandro Case; Enrico Cancellotti; Carlo Valente; Howard S Marsden; Giorgio Palù
Journal:  J Virol       Date:  2006-07       Impact factor: 5.103

4.  Mutations that specifically impair the DNA binding activity of the herpes simplex virus protein UL42.

Authors:  C S Chow; D M Coen
Journal:  J Virol       Date:  1995-11       Impact factor: 5.103

5.  Sequences at the C-terminus of the herpes simplex virus type 1 UL30 protein are dispensable for DNA polymerase activity but not for viral origin-dependent DNA replication.

Authors:  N D Stow
Journal:  Nucleic Acids Res       Date:  1993-01-11       Impact factor: 16.971

6.  Cloning, sequencing, and functional characterization of the two subunits of the pseudorabies virus DNA polymerase holoenzyme: evidence for specificity of interaction.

Authors:  H Berthomme; S J Monahan; D S Parris; B Jacquemont; A L Epstein
Journal:  J Virol       Date:  1995-05       Impact factor: 5.103

7.  Inhibition of human cytomegalovirus DNA polymerase by C-terminal peptides from the UL54 subunit.

Authors:  Arianna Loregian; Roberto Rigatti; Mary Murphy; Elisabetta Schievano; Giorgio Palu; Howard S Marsden
Journal:  J Virol       Date:  2003-08       Impact factor: 5.103

8.  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
  8 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.