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ATP-dependent unwinding of a minimal origin of DNA replication by the origin-binding protein and the single-strand DNA-binding protein ICP8 from herpes simplex virus type I.

Journal article
Authors Alireza Aslani
Monica Olsson
Per Elias
Published in The Journal of biological chemistry
Volume 277
Issue 43
Pages 41204-12
ISSN 0021-9258
Publication year 2002
Published at Institute of Medical Biochemistry
Pages 41204-12
Language en
Links dx.doi.org/10.1074/jbc.M208270200
Keywords Adenosine Triphosphate, metabolism, Base Sequence, DNA Footprinting, DNA-Binding Proteins, Nucleic Acid Conformation, Oligodeoxyribonucleotides, Replication Origin, Viral Proteins, metabolism
Subject categories Virology, Medical Biotechnology (with a focus on Cell Biology (including Stem Cell Biology), Molecular Biology, Microbiology, Biochemistry or Biopharmacy)

Abstract

The Herpes simplex virus type I origin-binding protein, OBP, is encoded by the UL9 gene. OBP binds the origin of DNA replication, oriS, in a cooperative and sequence-specific manner. OBP is also an ATP-dependent DNA helicase. We have recently shown that single-stranded oriS folds into a unique and evolutionarily conserved conformation, oriS*, which is stably bound by OBP. OriS* contains a stable hairpin formed by complementary base pairing between box I and box III in oriS. Here we show that OBP, in the presence of the single-stranded DNA-binding protein ICP8, can convert an 80-base pair double-stranded minimal oriS fragment to oriS* and form an OBP-oriS* complex. The formation of an OBP-oriS* complex requires hydrolysable ATP. We also demonstrate that OBP in the presence of ICP8 and ATP promotes slow but specific and complete unwinding of duplex minimal oriS. The possibility that the OBP-oriS* complex may serve as an assembly site for the herpes virus replisome is discussed.

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