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Functional properties of the herpes simplex virus type I origin-binding protein are controlled by precise interactions with the activated form of the origin of DNA replication.

Journal article
Authors Bertil Macao
Monica Olsson
Per Elias
Published in The Journal of biological chemistry
Volume 279
Issue 28
Pages 29211-7
ISSN 0021-9258
Publication year 2004
Published at Institute of Medical Biochemistry
Pages 29211-7
Language en
Links dx.doi.org/10.1074/jbc.M400371200
Keywords Adenosine Triphosphate, metabolism, Base Sequence, DNA, chemistry, metabolism, DNA Helicases, genetics, metabolism, DNA Repair Enzymes, DNA Replication, DNA-Binding Proteins, chemistry, genetics, metabolism, Escherichia coli Proteins, metabolism, Exodeoxyribonucleases, metabolism, Herpesvirus 1, Human, genetics, Macromolecular Substances, Models, Genetic, Molecular Sequence Data, Nucleic Acid Conformation, Protein Conformation, Replication Origin, Viral Proteins, chemistry, genetics, metabolism
Subject categories Medical and Health Sciences

Abstract

The herpes simplex virus, type I origin-binding protein, OBP, is a superfamily II DNA helicase encoded by the UL9 gene. OBP binds in a sequence-specific and cooperative way to the viral origin of replication oriS. OBP may unwind partially and introduce a hairpin into the double-stranded origin of replication. The formation of the novel conformation referred to as oriS* also requires the single-stranded DNA-binding protein, ICP8, and ATP hydrolysis. OBP forms a stable complex with oriS*. The hairpin in oriS* provides a site for sequence-specific attachment, and a single-stranded region triggers ATP hydrolysis. Here we use Escherichia coli exonuclease I to map the binding of the C-terminal domain of OBP to the hairpin and the helicase domains to the single-stranded tail. The helicase domains cover a stretch of 23 nucleotides of single-stranded DNA. Using streptavidin-coated magnetic beads, we show that OBP may bind two copies of double-stranded DNA (one biotin-labeled and the other one radioactively labeled) but only one copy of oriS*. It is the length of the single-stranded tail that determines the stoichiometry of OBP.DNA complexes. OBP interacts with the bases of the single-stranded tail, and ATP hydrolysis is triggered by position-specific interactions between OBP and bases in the single-stranded tail of oriS*.

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