ArticleNucleic acids research1992
Identification of a novel downstream binding protein implicated in late-phase-specific activation of the adenovirus major late promotor.
Article in Nucleic acids research, 1992. 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, 36 citations in OpenAlex.
- Understanding Post Entry Sorting of Adenovirus Capsids; A Chance to Change Vaccine Vector Properties.Viruses · 2021Review
- Adenovirus Core Proteins: Structure and Function.Viruses · 2021Review
- Regulation of human adenovirus alternative RNA splicing by the adenoviral L4-33K and L4-22K proteins.International journal of molecular sciences · 2015Review
- Adenovirus late-phase infection is controlled by a novel L4 promoter.Journal of virology · 2010Article
- Adenovirus serotype 5 L4-22K and L4-33K proteins have distinct functions in regulating late gene expression.Journal of virology · 2009Article
- The adenovirus L4 33-kilodalton protein binds to intragenic sequences of the major late promoter required for late phase-specific stimulation of transcription.Journal of virology · 2007Article
- The L4 22-kilodalton protein plays a role in packaging of the adenovirus genome.Journal of virology · 2006Article
- Functional interaction of the adenovirus IVa2 protein with adenovirus type 5 packaging sequences.Journal of virology · 2005Article
- Viral DNA synthesis-dependent titration of a cellular repressor activates transcription of the human adenovirus type 2 IVa2 gene.Proceedings of the National Academy of Sciences of the United States of America · 2004Article
- Requirement of the adenovirus IVa2 protein for virus assembly.Journal of virology · 2003Article
- Analysis of the adenovirus E1B-55K-anchored proteome reveals its link to ubiquitination machinery.Journal of virology · 2002Article
- Role for the adenovirus IVa2 protein in packaging of viral DNA.Journal of virology · 2001Article
- Interaction of the adenovirus IVa2 protein with viral packaging sequences.Journal of virology · 2000Article
- Encapsidation of viral DNA requires the adenovirus L1 52/55-kilodalton protein.Journal of virology · 1998Article
- Functional analysis of the CAAT box in the major late promoter of the subgroup C human adenoviruses.Journal of virology · 1998Article
- Nucleoplasmic and nucleolar distribution of the adenovirus IVa2 gene product.Journal of virology · 1996Article
- Properties of the adenovirus IVa2 gene product, an effector of late-phase-dependent activation of the major late promoter.Journal of virology · 1996Article
- The product of the adenovirus intermediate gene IVa2 is a transcriptional activator of the major late promoter.Journal of virology · 1994Article
- Sequences downstream of the RNA initiation site regulate human T-cell lymphotropic virus type I basal gene expression.Journal of virology · 1993Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The adenovirus major late promotor (MLP) is induced to very high levels after the onset of the viral DNA replication. Previous studies have identified sequence elements located downstream of the MLP startsite (DE1, between +85 and +98; DE2, between +100 and +120) implicated, together with the upstream promoter element, in this late-phase-specific transcriptional activation. One protein (DEF, now renamed DEF-A), induced during the late phase of viral infection, has been identified and shown to bind to the DE1 element (Jansen-Durr et al., 1989, J. Virol. 63, 5124-5132). Here we report about a distinct late-phase-specific protein (DEF-B) and its interactions with DEF-A. DNA-binding studies reveal that DEF-B interacts with the 5' part of DE2 (DE2b), whereas DEF-A, besides its interaction with DE1, also binds to the 3' portion of DE2 (DE2a), but with a lower affinity than for DE1. Furthermore, when added together, DEF-A and DEF-B cooperatively assemble onto the DE2 element as a heteromeric complex which is substantially more stable than the complexes formed by each protein alone. Using an in vivo transcriptional assay of the MLP, we show that DEF-A and DEF-B both have intrinsic transactivating properties.
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