Nucleoprotein complex formed between herpes simplex virus UL9 protein and the origin of DNA replication: Inter- and intramolecular interactions Journal Article

   


Authors: Rabkin, S. D.; Hanlon, B.
Article Title: Nucleoprotein complex formed between herpes simplex virus UL9 protein and the origin of DNA replication: Inter- and intramolecular interactions
Abstract: The UL9 gene of herpes simplex virus type 1 encodes an origin-binding protein. UL9 protein purified from baculovirus vector-infected insect cells forms a stable complex with DNA containing the herpes simplex virus origin of DNA replication, ori(s). Contained within ori(s) are two UL9 protein-binding sites, I and II, bracketing an (A+T)-rich region. UL9 protein, visualized by electron microscopy, binds selectively at the site of the origin and covers ≃120 base pairs. Upon formation of the nucleoprotein complex, the apparent contour length of the DNA is shortened, suggesting that this amount of DNA is wrapped or condensed by the protein. A nucleoprotein complex of similar size and structure forms on an inactive origin deleted for binding site II. Multiple intermolecular interactions occur. In particular, UL9 nucleoprotein complexes interact in trans with other UL9 nucleoprotein complexes such that dimer DNA molecules are formed with a junction at the position of protein binding. The DNA molecules in these intermolecular complexes are aligned predominantly in a parallel orientation.
Keywords: nonhuman; dna replication; electron microscopy; simplexvirus; dna replication origin; herpes simplex virus; herpes; fungus; fungi; virus protein; virus cell interaction; human herpesvirus 1; unidentified baculovirus; insecta; nucleoprotein; priority journal; article
Journal Title: Proceedings of the National Academy of Sciences of the United States of America
Volume: 88
Issue: 23
ISSN: 0027-8424
Publisher: National Academy of Sciences  
Date Published: 1991-12-01
Start Page: 10946
End Page: 10950
Language: English
DOI: 10.1073/pnas.88.23.10946
PUBMED: 1660157
PROVIDER: scopus
PMCID: PMC53049
DOI/URL:

https://www.scopus.com/inward/record.uri?eid=2-s2.0-0025721026&doi=10.1073%2fpnas.88.23.10946&partnerID=40&md5=7684ee1b64a6fab788a76dececc36eb3
Notes: Source: Scopus
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