ArticleJournal of molecular biology2009
The bipolar filaments formed by herpes simplex virus type 1 SSB/recombination protein (ICP8) suggest a mechanism for DNA annealing.
Article in Journal of molecular biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 26 citations in OpenAlex.
- Mechanism of single-strand annealing from native mass spectrometry and cryo-EM structures of RAD52 homolog Mgm101.Nucleic acids research · 2026Article
- Mechanism of single-strand annealing from native mass spectrometry and cryo-EM structures of RAD52 homolog Mgm101.bioRxiv : the preprint server for biology · 2025Article
- Half a century after their discovery: Structural insights into exonuclease and annealase proteins catalyzing recombineering.Engineering microbiology · 2024Review
- RedβNature communications · 2022Article
- Mutational Analysis of Redβ Single Strand Annealing Protein: Roles of the 14 Lysine Residues in DNA Binding and Recombination In Vivo.International journal of molecular sciences · 2021Article
- The three-component helicase/primase complex of herpes simplex virus-1.Open biology · 2021Review
- Structure and mechanism of the Red recombination system of bacteriophage λ.Progress in biophysics and molecular biology · 2019Review
- The UL8 subunit of the helicase-primase complex of herpes simplex virus promotes DNA annealing and has a high affinity for replication forks.The Journal of biological chemistry · 2017Article
- ICP8 Filament Formation Is Essential for Replication Compartment Formation during Herpes Simplex Virus Infection.Journal of virology · 2015Article
- DNA-pairing and annealing processes in homologous recombination and homology-directed repair.Cold Spring Harbor perspectives in biology · 2015Review
- Interaction of Kaposi's sarcoma-associated herpesvirus ORF6 protein with single-stranded DNA.Journal of virology · 2014Article
- Recombination promoted by DNA viruses: phage λ to herpes simplex virus.Annual review of microbiology · 2014Review
- Details of ssDNA annealing revealed by an HSV-1 ICP8-ssDNA binary complex.Nucleic acids research · 2013Article
- Are ParM filaments polar or bipolar?Journal of molecular biology · 2012Article
- Herpes simplex viruses: mechanisms of DNA replication.Cold Spring Harbor perspectives in biology · 2012Review
- Real-space processing of helical filaments in SPARX.Journal of structural biology · 2012Article
- Structure-function relationships of the competence lipoprotein ComL and SSB in meningococcal transformation.Microbiology (Reading, England) · 2011Article
- The Kaposi's sarcoma-associated herpesvirus ORF6 DNA binding protein forms long DNA-free helical protein filaments.Journal of structural biology · 2011Article
- Contributions of nucleotide excision repair, DNA polymerase eta, and homologous recombination to replication of UV-irradiated herpes simplex virus type 1.The Journal of biological chemistry · 2010Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
Abstract
Herpes simplex virus type 1 encodes a multifunctional protein, ICP8, which serves both as a single-strand binding protein and as a recombinase, catalyzing reactions involved in replication and recombination of the viral genome. In the presence of divalent ions and at low temperature, previous electron microscopic studies showed that ICP8 will form long left-handed helical filaments. Here, electron microscopic image reconstruction reveals that the filaments are bipolar, with an asymmetric unit containing two subunits of ICP8 that constitute a symmetrical dimer. This organization of the filament has been confirmed using scanning transmission electron microscopy. The pitch of the filaments is approximately 250 A, with approximately 6.2 dimers per turn. Docking of a crystal structure of ICP8 into the reconstructed filament shows that the C-terminal domain of ICP8, attached to the body of the subunit by a flexible linker containing approximately 10 residues, is packed into a pocket in the body of a neighboring subunit in the crystal in a similar manner as in the filament. However, the interactions between the large N-terminal domains are quite different in the filament from that observed in the crystal. A previously proposed model for ICP8 binding single-stranded DNA (ssDNA), based upon the crystal structure, leads to a model for a continuous strand of ssDNA near the filament axis. The bipolar nature of the ICP8 filaments means that a second strand of ssDNA would be running through this filament in the opposite orientation, and this provides a potential mechanism for how ICP8 anneals complementary ssDNA into double-stranded DNA, where each strand runs in opposite directions.
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