ArticleJournal of virology2006
Interactions among four proteins encoded by the human cytomegalovirus UL112-113 region regulate their intranuclear targeting and the recruitment of UL44 to prereplication foci.
Article in Journal of virology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed.
- G-quadruplex as an essential structural element in cytomegalovirus replication origin.Nature communications · 2024Article
- The Impact of Co-Infections for Human Gammaherpesvirus Infection and Associated Pathologies.International journal of molecular sciences · 2023Review
- Review
- Human cytomegalovirus forms phase-separated compartments at viral genomes to facilitate viral replication.Cell reports · 2022Article
- Dual infection and recombination of Kaposi sarcoma herpesvirus revealed by whole-genome sequence analysis of effusion samples.Virus evolution · 2020Article
- Infected T98G glioblastoma cells support human cytomegalovirus reactivation from latency.Virology · 2017Article
- Differential Requirement of Human Cytomegalovirus UL112-113 Protein Isoforms for Viral Replication.Journal of virology · 2017Article
- Functional Dissection of an Alternatively Spliced Herpesvirus Gene by Splice Site Mutagenesis.Journal of virology · 2016Article
- Co-infections and Pathogenesis of KSHV-Associated Malignancies.Frontiers in microbiology · 2016Review
- Requirement of the N-terminal residues of human cytomegalovirus UL112-113 proteins for viral growth and oriLyt-dependent DNA replication.Journal of microbiology (Seoul, Korea) · 2015Article
- Article
- A short cis-acting motif in the M112-113 promoter region is essential for IE3 to activate M112-113 gene expression and is important for murine cytomegalovirus replication.Journal of virology · 2013Article
- A novel bat herpesvirus encodes homologues of major histocompatibility complex classes I and II, C-type lectin, and a unique family of immune-related genes.Journal of virology · 2012Article
- Depletion of cellular pre-replication complex factors results in increased human cytomegalovirus DNA replication.PloS one · 2012Article
- Yeast two hybrid analyses reveal novel binary interactions between human cytomegalovirus-encoded virion proteins.PloS one · 2011Article
- Identification of binary interactions between human cytomegalovirus virion proteins.Journal of virology · 2011Article
- Role of the specific interaction of UL112-113 p84 with UL44 DNA polymerase processivity factor in promoting DNA replication of human cytomegalovirus.Journal of virology · 2010Article
- Mutations in the M112/M113-coding region facilitate murine cytomegalovirus replication in human cells.Journal of virology · 2010Article
- Role of noncovalent SUMO binding by the human cytomegalovirus IE2 transactivator in lytic growth.Journal of virology · 2010Article
- Tegument proteins of human cytomegalovirus.Microbiology and molecular biology reviews : MMBR · 2008Review
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6 authors.
Funding
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Abstract
Four phosphoproteins, of 34, 43, 50, and 84 kDa, with common amino termini are synthesized via alternative splicing from the UL112-113 region of the human cytomegalovirus genome. Although genetic studies provided evidence that both the UL112 and UL113 loci in the viral genome are required for efficient viral replication, whether the four proteins play specific roles or cooperate in replication is not understood. Here we present evidence, using in vitro and in vivo coimmunoprecipitation assays, that the four UL112-113 proteins both self-interact and interact with each other. A mapping study of the 84-kDa protein showed that the N-terminal region encompassing amino acids 1 to 125, which is shared in all UL112-113 proteins and highly conserved among betaherpesviruses, is required for both self-interaction and nuclear localization as foci. Further localization studies revealed that, unlike the 43-, 50-, and 84-kDa proteins, which were distributed as nuclear punctate forms, the 34-kDa form was located predominantly in the cytoplasm. However, when all four proteins were coexpressed simultaneously, all of the UL112-113 proteins were efficiently localized to the promyelocytic leukemia oncogenic domains. We also found that the ability of the UL112-113 proteins to relocate UL44 (the viral polymerase processivity factor) to prereplication foci relied on self-interaction and reached maximal levels when the four proteins were coexpressed. Therefore, our data suggest that interactions occurring among UL112-113 proteins via their shared N-terminal regions are important to both their intranuclear targeting and the recruitment of UL44 to subnuclear sites for viral replication.
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