ArticleJournal of virology2000
A chimeric protein containing the N terminus of the adeno-associated virus Rep protein recognizes its target site in an in vivo assay.
Article in Journal of virology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed.
- The Expression and Function of the Small Nonstructural Proteins of Adeno-Associated Viruses (AAVs).Viruses · 2024Review
- Adeno-Associated Virus Genome Interactions Important for Vector Production and Transduction.Human gene therapy · 2020Review
- Article
- Rescue of DNA-PK Signaling and T-Cell Differentiation by Targeted Genome Editing in a prkdc Deficient iPSC Disease Model.PLoS genetics · 2015Article
- Retargeting sleeping beauty transposon insertions by engineered zinc finger DNA-binding domains.Molecular therapy : the journal of the American Society of Gene Therapy · 2012Article
- Retargeting transposon insertions by the adeno-associated virus Rep protein.Nucleic acids research · 2012Article
- The interdomain linker of AAV-2 Rep68 is an integral part of its oligomerization domain: role of a conserved SF3 helicase residue in oligomerization.PLoS pathogens · 2012Article
- Formation of AAV single stranded DNA genome from a circular plasmid in Saccharomyces cerevisiae.PloS one · 2011Article
- Integration preferences of wildtype AAV-2 for consensus rep-binding sites at numerous loci in the human genome.PLoS pathogens · 2010Article
- Transcriptional analysis of the adeno-associated virus integration site.Journal of virology · 2009Article
- Efficient expression of the adeno-associated virus type 5 p41 capsid gene promoter in 293 cells does not require Rep.Journal of virology · 2006Article
- The cellular TATA binding protein is required for rep-dependent replication of a minimal adeno-associated virus type 2 p5 element.Journal of virology · 2005Article
- Structure of adeno-associated virus type 2 Rep40-ADP complex: insight into nucleotide recognition and catalysis by superfamily 3 helicases.Proceedings of the National Academy of Sciences of the United States of America · 2004Article
- The adeno-associated virus type 2 Rep protein regulates RNA processing via interaction with the transcription template.Molecular and cellular biology · 2002Article
- A genetic screen identifies a cellular regulator of adeno-associated virus.Proceedings of the National Academy of Sciences of the United States of America · 2001Article
- A functional complex of adenovirus proteins E1B-55kDa and E4orf6 is necessary to modulate the expression level of p53 but not its transcriptional activity.Journal of virology · 2000Article
Corrections and comments
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The Rep78 and Rep68 proteins of adeno-associated virus (AAV) type 2 are involved in DNA replication, regulation of gene expression, and targeting site-specific integration. They bind to a specific Rep recognition sequence (RRS) found in both the viral inverted terminal repeats and the AAVS1 integration locus on human chromosome 19. Previous in vitro studies implied that an N-terminal segment of Rep is involved in DNA recognition, while additional domains might stabilize binding and mediate multimerization. In order to define the minimal requirements for Rep to recognize its target site in the human genome, we developed one-hybrid assays in which DNA-protein interactions are detected in vivo. Chimeric proteins consisting of the N terminus of Rep fused to different oligomerization motifs and a transcriptional activation domain were analyzed for oligomerization, DNA binding, and activation of reporter gene expression. Expression of reporter genes was driven from RRS motifs cloned upstream of minimal promoters and examined in mammalian cells from transfected plasmids and in Saccharomyces cerevisiae from a reporter cassette integrated into the yeast genome. Our results show for the first time that chimeric proteins containing the amino-terminal 244 residues of Rep are able to target the RRS in vitro and in vivo when incorporated into artificial multimers. These studies suggest that chimeric proteins may be used to harness the unique targeting feature of AAV for gene therapy applications.
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