Previous Article | Next Article 
J Virol. 1990 December; 64(12): 5976-5987
The herpes simplex virus type 1 UL42 gene product: a subunit of DNA polymerase that functions to increase processivity.
J Gottlieb,
A I Marcy,
D M Coen and
M D Challberg
Laboratory of Viral Diseases, National Institute of Allergy and Infectious Diseases, Bethesda, Maryland 20892.
ABSTRACT
Genetic experiments have shown that the products of the herpes simplex virus type 1 (HSV-1) DNA polymerase (UL30) and UL42 genes are both required for viral DNA replication, and a number of studies have suggested that these two proteins specifically interact. We have confirmed and extended these findings. The viral DNA polymerase from HSV-1-infected cells has been purified as a complex containing equimolar quantities of the UL30 (Pol, the catalytic subunit) and UL42 polypeptides. Sedimentation and gel filtration analyses of this complex are consistent with the idea that the complex consists of a heterodimer of Pol and UL42. A complex with identical physical and functional properties was also purified from insect cells coinfected with recombinant baculoviruses expressing the two polypeptides. Therefore, the formation of the Pol-UL42 complex does not require the participation of any other HSV-encoded protein. We have compared the catalytic properties of the Pol-UL42 complex with those of the isolated subunits of the enzyme purified from recombinant baculovirus-infected insect cells. The specific activity of the catalytic subunit alone was nearly identical to that of the complex when assayed on activated DNA. When assayed on a defined template such as singly primed M13 DNA, however, the combination of Pol and UL42 utilized fewer primers and formed larger products than Pol alone. Template challenge experiments demonstrated that the Pol-UL42 complex was more highly processive than Pol alone. Our data are consistent with the idea that the UL42 polypeptide is an accessory subunit of the DNA polymerase that acts to increase the processivity of polymerization.
J Virol. 1990 December; 64(12): 5976-5987
This article has been cited by other articles:
-
Tian, W., Hwang, Y. T., Hwang, C. B. C.
(2008). The Enhanced DNA Replication Fidelity of a Mutant Herpes Simplex Virus Type 1 DNA Polymerase Is Mediated by an Improved Nucleotide Selectivity and Reduced Mismatch Extension Ability. J. Virol.
82: 8937-8941
[Abstract]
[Full Text]
-
Smith-Donald, B. A., Durand, L. O., Roizman, B.
(2008). Role of Cellular Phosphatase cdc25C in Herpes Simplex Virus 1 Replication. J. Virol.
82: 4527-4532
[Abstract]
[Full Text]
-
Komazin-Meredith, G., Santos, W. L., Filman, D. J., Hogle, J. M., Verdine, G. L., Coen, D. M.
(2008). The Positively Charged Surface of Herpes Simplex Virus UL42 Mediates DNA Binding. J. Biol. Chem.
283: 6154-6161
[Abstract]
[Full Text]
-
Jiang, C., Hwang, Y. T., Wang, G., Randell, J. C. W., Coen, D. M., Hwang, C. B. C.
(2007). Herpes Simplex Virus Mutants with Multiple Substitutions Affecting DNA Binding of UL42 Are Impaired for Viral Replication and DNA Synthesis. J. Virol.
81: 12077-12079
[Abstract]
[Full Text]
-
Link, M. A., Silva, L. A., Schaffer, P. A.
(2007). Cathepsin B Mediates Cleavage of Herpes Simplex Virus Type 1 Origin Binding Protein (OBP) To Yield OBPC-1, and Cleavage Is Dependent upon Viral DNA Replication. J. Virol.
81: 9175-9182
[Abstract]
[Full Text]
-
Hanes, J. W., Zhu, Y., Parris, D. S., Johnson, K. A.
(2007). Enzymatic Therapeutic Index of Acyclovir: VIRAL VERSUS HUMAN POLYMERASE {gamma} SPECIFICITY. J. Biol. Chem.
282: 25159-25167
[Abstract]
[Full Text]
-
Loregian, A., Sinigalia, E., Mercorelli, B., Palu, G., Coen, D. M.
(2007). Binding parameters and thermodynamics of the interaction of the human cytomegalovirus DNA polymerase accessory protein, UL44, with DNA: implications for the processivity mechanism. Nucleic Acids Res
35: 4779-4791
[Abstract]
[Full Text]
-
Jiang, C., Hwang, Y. T., Randell, J. C. W., Coen, D. M., Hwang, C. B. C.
(2007). Mutations That Decrease DNA Binding of the Processivity Factor of the Herpes Simplex Virus DNA Polymerase Reduce Viral Yield, Alter the Kinetics of Viral DNA Replication, and Decrease the Fidelity of DNA Replication. J. Virol.
81: 3495-3502
[Abstract]
[Full Text]
-
Loregian, A., Case, A., Cancellotti, E., Valente, C., Marsden, H. S., Palu, G.
(2006). Cloning, expression, and functional characterization of the equine herpesvirus 1 DNA polymerase and its accessory subunit.. J. Virol.
80: 6247-6258
[Abstract]
[Full Text]
-
Appleton, B. A., Brooks, J., Loregian, A., Filman, D. J., Coen, D. M., Hogle, J. M.
(2006). Crystal Structure of the Cytomegalovirus DNA Polymerase Subunit UL44 in Complex with the C Terminus from the Catalytic Subunit: DIFFERENCES IN STRUCTURE AND FUNCTION RELATIVE TO UNLIGANDED UL44. J. Biol. Chem.
281: 5224-5232
[Abstract]
[Full Text]
-
Randell, J. C. W., Komazin, G., Jiang, C., Hwang, C. B. C., Coen, D. M.
(2005). 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. J. Virol.
79: 12025-12034
[Abstract]
[Full Text]
-
Loregian, A., Appleton, B. A., Hogle, J. M., Coen, D. M.
(2004). Specific Residues in the Connector Loop of the Human Cytomegalovirus DNA Polymerase Accessory Protein UL44 Are Crucial for Interaction with the UL54 Catalytic Subunit. J. Virol.
78: 9084-9092
[Abstract]
[Full Text]
-
Chen, X., Lin, K., Ricciardi, R. P.
(2004). Human Kaposi's Sarcoma Herpesvirus Processivity Factor-8 Functions as a Dimer in DNA Synthesis. J. Biol. Chem.
279: 28375-28386
[Abstract]
[Full Text]
-
Wang, Y., Prosen, D. E., Mei, L., Sullivan, J. C., Finney, M., Vander Horn, P. B.
(2004). A novel strategy to engineer DNA polymerases for enhanced processivity and improved performance in vitro. Nucleic Acids Res
32: 1197-1207
[Abstract]
[Full Text]
-
Loregian, A., Appleton, B. A., Hogle, J. M., Coen, D. M.
(2004). Residues of Human Cytomegalovirus DNA Polymerase Catalytic Subunit UL54 That Are Necessary and Sufficient for Interaction with the Accessory Protein UL44. J. Virol.
78: 158-167
[Abstract]
[Full Text]
-
Loregian, A., Rigatti, R., Murphy, M., Schievano, E., Palu, G., Marsden, H. S.
(2003). Inhibition of Human Cytomegalovirus DNA Polymerase by C-Terminal Peptides from the UL54 Subunit. J. Virol.
77: 8336-8344
[Abstract]
[Full Text]
-
Chaudhuri, M., Song, L., Parris, D. S.
(2003). The Herpes Simplex Virus Type 1 DNA Polymerase Processivity Factor Increases Fidelity without Altering Pre-steady-state Rate Constants for Polymerization or Excision. J. Biol. Chem.
278: 8996-9004
[Abstract]
[Full Text]
-
Das, A., Bellofatto, V.
(2003). From the Cover: RNA polymerase II-dependent transcription in trypanosomes is associated with a SNAP complex-like transcription factor. Proc. Natl. Acad. Sci. USA
100: 80-85
[Abstract]
[Full Text]
-
Chaudhuri, M., Parris, D. S.
(2002). Evidence against a Simple Tethering Model for Enhancement of Herpes Simplex Virus DNA Polymerase Processivity by Accessory Protein UL42. J. Virol.
76: 10270-10281
[Abstract]
[Full Text]
-
Thomas, S. K., Lilley, C. E., Latchman, D. S., Coffin, R. S.
(2002). A Protein Encoded by the Herpes Simplex Virus (HSV) Type 1 2-Kilobase Latency-Associated Transcript Is Phosphorylated, Localized to the Nucleus, and Overcomes the Repression of Expression from Exogenous Promoters When Inserted into the Quiescent HSV Genome. J. Virol.
76: 4056-4067
[Abstract]
[Full Text]
-
Gershburg, E., Pagano, J. S.
(2002). Phosphorylation of the Epstein-Barr Virus (EBV) DNA Polymerase Processivity Factor EA-D by the EBV-Encoded Protein Kinase and Effects of the L-Riboside Benzimidazole 1263W94. J. Virol.
76: 998-1003
[Abstract]
[Full Text]
-
Klemperer, N., McDonald, W., Boyle, K., Unger, B., Traktman, P.
(2001). The A20R Protein Is a Stoichiometric Component of the Processive Form of Vaccinia Virus DNA Polymerase. J. Virol.
75: 12298-12307
[Abstract]
[Full Text]
-
Chan, S. R., Chandran, B.
(2000). Characterization of Human Herpesvirus 8 ORF59 Protein (PF-8) and Mapping of the Processivity and Viral DNA Polymerase-Interacting Domains. J. Virol.
74: 10920-10929
[Abstract]
[Full Text]
-
Sampson, D. A., Arana, M. E., Boehmer, P. E.
(2000). Cysteine 111 Affects Coupling of Single-stranded DNA Binding to ATP Hydrolysis in the Herpes Simplex Virus Type-1 Origin-binding Protein. J. Biol. Chem.
275: 2931-2937
[Abstract]
[Full Text]
-
Bridges, K. G., Hua, Q., Brigham-Burke, M. R., Martin, J. D., Hensley, P., Dahl, C. E., Digard, P., Weiss, M. A., Coen, D. M.
(2000). Secondary Structure and Structure-Activity Relationships of Peptides Corresponding to the Subunit Interface of Herpes Simplex Virus DNA Polymerase. J. Biol. Chem.
275: 472-478
[Abstract]
[Full Text]
-
Lehman, I. R., Boehmer, P. E.
(1999). Replication of Herpes Simplex Virus DNA. J. Biol. Chem.
274: 28059-28062
[Full Text]
-
Fan, L., Sanschagrin, P. C., Kaguni, L. S., Kuhn, L. A.
(1999). The accessory subunit of mtDNA polymerase shares structural homology with aminoacyl-tRNA synthetases: Implications for a dual role as a primer recognition factor and processivity clamp. Proc. Natl. Acad. Sci. USA
96: 9527-9532
[Abstract]
[Full Text]
-
McDougal, V. V., Guarino, L. A.
(1999). Autographa californica Nuclear Polyhedrosis Virus DNA Polymerase: Measurements of Processivity and Strand Displacement. J. Virol.
73: 4908-4918
[Abstract]
[Full Text]
-
Loregian, A., Papini, E., Satin, B., Marsden, H. S., Hirst, T. R., Palu, G.
(1999). Intranuclear delivery of an antiviral peptide mediated by the B subunit of Escherichia coli heat-labile enterotoxin. Proc. Natl. Acad. Sci. USA
96: 5221-5226
[Abstract]
[Full Text]
-
Matković-Calogović, D., Loregian, A., D'Acunto, M. R., Battistutta, R., Tossi, A., Palu, G., Zanotti, G.
(1999). Crystal Structure of the B Subunit of Escherichia coli Heat-labile Enterotoxin Carrying Peptides with Anti-herpes Simplex Virus Type 1 Activity. J. Biol. Chem.
274: 8764-8769
[Abstract]
[Full Text]
-
Huang, L., Ishii, K. K., Zuccola, H., Gehring, A. M., Hwang, C. B. C., Hogle, J., Coen, D. M.
(1999). The enzymological basis for resistance of herpesvirus DNA polymerase mutants to acyclovir: Relationship to the structure of alpha -like DNA polymerases. Proc. Natl. Acad. Sci. USA
96: 447-452
[Abstract]
[Full Text]
-
Weisshart, K., Chow, C. S., Coen, D. M.
(1999). 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. J. Virol.
73: 55-66
[Abstract]
[Full Text]
-
Falkenberg, M., Elias, P., Lehman, I. R.
(1998). The Herpes Simplex Virus Type 1 Helicase-primase. ANALYSIS OF HELICASE ACTIVITY. J. Biol. Chem.
273: 32154-32157
[Abstract]
[Full Text]
-
Spector, F. C., Liang, L., Giordano, H., Sivaraja, M., Peterson, M. G.
(1998). Inhibition of Herpes Simplex Virus Replication by a 2-Amino Thiazole via Interactions with the Helicase Component of the UL5-UL8-UL52 Complex. J. Virol.
72: 6979-6987
[Abstract]
[Full Text]
-
Lin, K., Dai, C. Y., Ricciardi, R. P.
(1998). Cloning and Functional Analysis of Kaposi's Sarcoma-Associated Herpesvirus DNA Polymerase and Its Processivity Factor. J. Virol.
72: 6228-6232
[Abstract]
[Full Text]
-
Dudas, K. C., Ruyechan, W. T.
(1998). Identification of a Region of the Herpes Simplex Virus Single-Stranded DNA-Binding Protein Involved in Cooperative Binding. J. Virol.
72: 257-265
[Abstract]
[Full Text]
-
Falkenberg, M., Bushnell, D. A., Elias, P., Lehman, I. R.
(1997). The UL8 Subunit of the Heterotrimeric Herpes Simplex Virus Type 1 Helicase-Primase Is Required for the Unwinding of Single Strand DNA-binding Protein (ICP8)-coated DNA Substrates. J. Biol. Chem.
272: 22766-22770
[Abstract]
[Full Text]
-
Kuhn, F. J.P., Knopf, C. W.
(1996). Herpes Simplex Virus Type 1DNA Polymerase. MUTATIONAL ANALYSIS OF THE 3prime -5prime -EXONUCLEASE DOMAIN. J. Biol. Chem.
271: 29245-29254
[Abstract]
[Full Text]
-
Almiron, M, Link, A J, Furlong, D, Kolter, R
(1992). A novel DNA-binding protein with regulatory and protective roles in starved Escherichia coli.. Genes Dev.
6: 2646-2654
[Abstract]
Copyright © 1990 by the American Society for Microbiology. All rights reserved.