The Host-Cell Architectural Protein HMG I(Y) Modulates Binding of Herpes Simplex Virus Type 1 ICP4 to Its Cognate Promoter

The productive infection cycle of herpes simplex virus is controlled in part by the action of ICP4, an immediate-early gene product that acts as both an activator and repressor of transcription. ICP4 is autoregulatory, and IE-3, the gene that encodes it, contains a high-affinity binding site for the...

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Bibliographic Details
Published in:Virology (New York, N.Y.) N.Y.), 1999-03, Vol.256 (1), p.64-74
Main Authors: Panagiotidis, Christos A., Silverstein, Saul J.
Format: Article
Language:English
Subjects:
Animals
Cell Nucleus - metabolism
Cercopithecus aethiops
DNA-Binding Proteins - genetics
DNA-Binding Proteins - metabolism
Gene Expression Regulation, Viral
Gene Library
HeLa Cells
Herpes simplex virus 1
Herpesvirus 1, Human - genetics
Herpesvirus 1, Human - physiology
High Mobility Group Proteins - genetics
High Mobility Group Proteins - metabolism
HMGA1a Protein
Humans
Immediate-Early Proteins - genetics
Immediate-Early Proteins - metabolism
Kinetics
Luciferases - genetics
Promoter Regions, Genetic
Recombinant Fusion Proteins - biosynthesis
Transcription Factors - genetics
Transcription Factors - metabolism
Transfection
Vero Cells
Virus Replication
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Summary:The productive infection cycle of herpes simplex virus is controlled in part by the action of ICP4, an immediate-early gene product that acts as both an activator and repressor of transcription. ICP4 is autoregulatory, and IE-3, the gene that encodes it, contains a high-affinity binding site for the protein at its cap site. Previously, we had demonstrated that this site could be occupied by proteins found in nuclear extracts from uninfected cells. A HeLa cell cDNA expression library was screened with a DNA probe containing the IE-3 gene cap site, and clones expressing the architectural chromatin proteins HMG I and HMG Y were identified by this technique. HMG I is shown to augment binding of ICP4 to its cognate site inin vitroassays and to enhance the activity of this protein in short-term transient expression assays.
ISSN:0042-6822
1096-0341
DOI:10.1006/viro.1999.9607