J Gen Virol Try Microbiology Online
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


J Gen Virol 64 (1983), 983-995; DOI 10.1099/0022-1317-64-5-983
© 1983 Society for General Microbiology

This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via CrossRef
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Littler, E.
Right arrow Articles by Powell, K. L.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Littler, E.
Right arrow Articles by Powell, K. L.
Agricola
Right arrow Articles by Littler, E.
Right arrow Articles by Powell, K. L.

Herpes Simplex Virus Non-structural Proteins. III. Function of the Major DNA-binding Protein

Edward Littler{dagger}, Dorothy Purifoy, Anthony Minson1 and Kenneth L. Powell

Department of Microbiology, University of Leeds, Leeds LS2 9JT, U.K.
and1 Department of Pathology, University of Cambridge, Laboratories Block, Addenbrooke's Hospital, Hills Road, Cambridge CB1 2QQ, U.K.

The herpes simplex virus type 2 major DNA-binding protein has been functionally characterized using temperature-sensitive mutants in the complementation group 2-2. The mutants were shown to be defective in the DNA-binding protein gene by mapping the mutants to the area of the genome known to code for the protein, and by demonstrating alterations in the major DNA-binding protein induced in mutant-infected cells. The mutants were shown to be defective in the replication of virus DNA. The nature of this defect was examined by studying virus DNA synthesis in vitro and by the examination of virus enzymes. An effect of mutation in the DNA-binding protein was to destabilize both the DNA polymerase and the alkaline exonuclease.

Keywords: HSV, DNA-binding proteins, ts mutants, protein function

{dagger} Present address: Department of Pathology, McMaster University, Hamilton, Ontario, Canada.

Received 15 November 1982; accepted 30 December 1982.


This article has been cited by other articles:


Home page
J. Gen. Virol.Home page
H. Lauterbach, C. Ried, A. L. Epstein, P. Marconi, and T. Brocker
Reduced immune responses after vaccination with a recombinant herpes simplex virus type 1 vector in the presence of antiviral immunity
J. Gen. Virol., September 1, 2005; 86(9): 2401 - 2410.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
I. Gascon, J. L. Carrascosa, L. Villar, J. M. Lazaro, and M. Salas
Importance of the N-terminal Region of the Phage GA-1 Single-stranded DNA-binding Protein for Its Self-interaction Ability and Functionality
J. Biol. Chem., June 14, 2002; 277(25): 22534 - 22540.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
N. T. Le Gac, G. Villani, and P. E. Boehmer
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
J. Biol. Chem., May 29, 1998; 273(22): 13801 - 13807.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
P. E. Boehmer
The Herpes Simplex Virus Type-1 Single-strand DNA-binding Protein, ICP8, Increases the Processivity of the UL9 Protein DNA Helicase
J. Biol. Chem., January 30, 1998; 273(5): 2676 - 2683.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
INT J SYST EVOL MICROBIOL MICROBIOLOGY J GEN VIROL
J MED MICROBIOL ALL SGM JOURNALS
Copyright © 1983 by the Society for General Microbiology.