ArticleProceedings of the National Academy of Sciences of the United States of America2001
Complementary intrastrand base pairing during initiation of Herpes simplex virus type 1 DNA replication.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 21 citations in OpenAlex.
- The herpes simplex origin-binding protein: mechanisms for sequence-specific DNA binding and dimerization revealed by Cryo-EM.Nucleic acids research · 2025Article
- Complex of the herpes simplex virus type 1 origin binding protein UL9 with DNA as a platform for the design of a new type of antiviral drugs.Journal of biomolecular structure & dynamics · 2014Article
- Sequencing of bovine herpesvirus 4 v.test strain reveals important genome features.Virology journal · 2011Article
- Evidence for DNA hairpin recognition by Zta at the Epstein-Barr virus origin of lytic replication.Journal of virology · 2010Article
- Initiation of lytic DNA replication in Epstein-Barr virus: search for a common family mechanism.Future virology · 2010Article
- Stepwise evolution of the herpes simplex virus origin binding protein and origin of replication.The Journal of biological chemistry · 2009Article
- Structural and biophysical characterization of the proteins interacting with the herpes simplex virus 1 origin of replication.The Journal of biological chemistry · 2009Article
- The herpes simplex virus type 1 DNA polymerase processivity factor, UL42, does not alter the catalytic activity of the UL9 origin-binding protein but facilitates its loading onto DNA.Nucleic acids research · 2005Article
- Functional interaction between the herpes simplex virus type 1 polymerase processivity factor and origin-binding proteins: enhancement of UL9 helicase activity.Journal of virology · 2003Article
- Antiviral and cytotoxic activity of netropsin derivatives in vero cells infected with vaccinia virus and herpes simplex virus type I.Doklady. Biochemistry and biophysicsArticle
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4 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
The herpes simplex virus type 1 origin of DNA replication, oriS, contains three copies of the recognition sequence for the viral initiator protein, origin binding protein (OBP), arranged in two palindromes. The central box I forms a short palindrome with box III and a long palindrome with box II. Single-stranded oriS adopts a conformation, oriS*, that is tightly bound by OBP. Here we demonstrate that OBP binds to a box III-box I hairpin with a 3' single-stranded tail in oriS*. Mutations designed to destabilize the hairpin abolish the binding of OBP to oriS*. The same mutations also inhibit DNA replication. Second site complementary mutations restore binding of OBP to oriS* as well as the ability of mutated oriS to support DNA replication. OriS* is also an efficient activator of the hydrolysis of ATP by OBP. Sequence analyses show that a box III-box I palindrome is an evolutionarily conserved feature of origins of DNA replication from human, equine, bovine, and gallid alpha herpes viruses. We propose that oriS facilitates initiation of DNA synthesis in two steps and that OBP exhibits exquisite specificity for the different conformations oriS adopts at these stages. Our model suggests that distance-dependent cooperative binding of OBP to boxes I and II in duplex DNA is succeeded by specific recognition of a box III-box I hairpin in partially unwound DNA.
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