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PMID: 1658370 Published · ppublish English Comparative Study Journal Article Research Support, Non-U.S. Gov't

Sequence, function, and regulation of the Vmw65 gene of herpes simplex virus type 2.

Journal of virology ·Vol. 65 ·No. 12 ·1991-12-00 ·Pages 6705-13

Greaves RF, O'Hare P

Abstract

We determined the sequence of the gene for the virion transactivator protein Vmw65 of herpes simplex virus type 2 (HSV-2), strain 333. An analysis of the coding sequence revealed an overall high degree of primary sequence conservation (86%) relative to the HSV-1 protein, although the carboxy-terminal region which encompasses the powerful acidic transactivation domain of the HSV-1 protein was slightly less well conserved (70%). One important change in this region was the presence of a proline residue in a region of the HSV-2 protein which is thought to form an amphipathic alpha-helix in the HSV-1 homolog. Despite the occurrence of this helix-disrupting residue, the HSV-2 protein exhibited powerful transactivation properties for immediate-early target promoters. We also demonstrated that the HSV-2 protein forms a transcriptional complex (TRF.C) with the cellular Oct-1 protein and target TAATGARAT elements from immediate-early promoters. A comparison of upstream sequences from the two Vmw65 genes revealed good conservation of proximal promoter elements but considerable divergence elsewhere. Specifically, the HSV-2 promoter alone carries 9.5 copies of a 9-bp direct repeat (GGGGCGGGA) ending 85 bp upstream of the conserved TTAAAT element. An analysis of transcription factor binding sites in vitro revealed that cellular factor Sp1 bound to the direct repeat sequence of the HSV-2 promoter and that cellular factor USF bound to a proximal element present in both HSV-1 and HSV-2 promoters. Mutational analysis of the HSV-2 promoter demonstrated that the integrity of both of these binding sites was important for the full activity of the promoter.

Related Genes
MeSH Terms
Amino Acid Sequence Animals Base Sequence Cell Line Cell Nucleus/metabolism Chloramphenicol O-Acetyltransferase/genetics,metabolism Gene Expression Regulation, Viral HeLa Cells Humans Kinetics Molecular Sequence Data Mutagenesis, Site-Directed Oligodeoxyribonucleotides Plasmids Restriction Mapping Sequence Homology, Nucleic Acid Simplexvirus/genetics Trans-Activators/genetics Transcriptional Activation Vero Cells Viral Proteins
Chemicals
Oligodeoxyribonucleotides Trans-Activators Viral Proteins Chloramphenicol O-Acetyltransferase
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Greaves R F
Marie Curie Research Institute, Oxted, Surrey, United Kingdom.
O'Hare P
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Article Info
Journal
Journal of virology
Abbr.
J Virol
ISSN
0022-538X
Published
1991-12-00
Pages
6705-13
Language
English
Region
United States
NLM ID
0113724
PMCID
PMC250747
Subset
IM
Databases
GENBANK
M64578, M64579, M64580, M64581, M64582, M64583, M74720, M75098, S59503, S59651
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