ArticleJournal of virology2013
Oligomeric properties of adeno-associated virus Rep68 reflect its multifunctionality.
Article in Journal of virology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed.
- Distinct YY dinucleotide periodicity in adeno-associated virus DNA.Molecular therapy : the journal of the American Society of Gene Therapy · 2026Article
- Insights into the AAV packaging mechanism: Cryo-EM Structure of the AAV2 Rep-Capsid Packaging Complex.bioRxiv : the preprint server for biology · 2025Article
- Article
- Cryo-EM structure of AAV2 Rep68 bound to integration site AAVS1: insights into the mechanism of DNA melting.Nucleic acids research · 2025Article
- Parvoviruses NS1 oncolytic attributes: mechanistic insights and synergistic anti-tumor therapeutic strategies.Frontiers in microbiology · 2025Review
- Cryo-EM Structure of AAV2 Rep68 bound to integration site AAVS1: Insights into the mechanism of DNA melting.bioRxiv : the preprint server for biology · 2024Article
- Inducible HEK293 AAV packaging cell lines expressing Rep proteins.Molecular therapy. Methods & clinical development · 2023Article
- Structure and function of the parvoviral NS1 protein: a review.Virus genes · 2023Review
- Next Step in Gene Delivery: Modern Approaches and Further Perspectives of AAV Tropism Modification.Pharmaceutics · 2021Review
- The Cryo-EM structure of AAV2 Rep68 in complex with ssDNA reveals a malleable AAA+ machine that can switch between oligomeric states.Nucleic acids research · 2020Article
- Adeno-Associated Virus Genome Interactions Important for Vector Production and Transduction.Human gene therapy · 2020Review
- Exchange of functional domains between a bacterial conjugative relaxase and the integrase of the human adeno-associated virus.PloS one · 2018Article
- Impact of Inverted Terminal Repeat Integrity on rAAV8 Production Using the Baculovirus/Sf9 Cells System.Human gene therapy methods · 2017Article
- Novel Mutant AAV2 Rep Proteins Support AAV2 Replication without Blocking HSV-1 Helpervirus Replication.PloS one · 2017Article
- DNA Binding and Cleavage by the Human Parvovirus B19 NS1 Nuclease Domain.Biochemistry · 2016Article
- Identification of a Functionally Relevant Adeno-Associated Virus Rep68 Oligomeric Interface.Journal of virology · 2016Article
- Conformational plasticity of RepB, the replication initiator protein of promiscuous streptococcal plasmid pMV158.Scientific reports · 2016Article
- Structural Insights into the Assembly of the Adeno-associated Virus Type 2 Rep68 Protein on the Integration Site AAVS1.The Journal of biological chemistry · 2015Article
- Adeno-Associated Virus Type 2 Rep68 Can Bind to Consensus Rep-Binding Sites on the Herpes Simplex Virus 1 Genome.Journal of virology · 2015Article
- Structural Studies of AAV2 Rep68 Reveal a Partially Structured Linker and Compact Domain Conformation.Biochemistry · 2015Article
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Authors and funding
9 authors.
Funding
Abstract
The adeno-associated virus (AAV) encodes four regulatory proteins called Rep. The large AAV Rep proteins Rep68 and Rep78 are essential factors required in almost every step of the viral life cycle. Structurally, they share two domains: a modified version of the AAA(+) domain that characterizes the SF3 family of helicases and an N-terminal domain that binds DNA specifically. The combination of these two domains imparts extraordinary multifunctionality to work as initiators of DNA replication and regulators of transcription, in addition to their essential role during site-specific integration. Although most members of the SF3 family form hexameric rings in vitro, the oligomeric nature of Rep68 is unclear due to its propensity to aggregate in solution. We report here a comprehensive study to determine the oligomeric character of Rep68 using a combination of methods that includes sedimentation velocity ultracentrifugation, electron microscopy, and hydrodynamic modeling. We have determined that residue Cys151 induces Rep68 to aggregate in vitro. We show that Rep68 displays a concentration-dependent dynamic oligomeric behavior characterized by the presence of two populations: one with monomers and dimers in slow equilibrium and a second one consisting of a mixture of multiple-ring structures of seven and eight members. The presence of either ATP or ADP induces formation of larger complexes formed by the stacking of multiple rings. Taken together, our results support the idea of a Rep68 molecule that exhibits the flexible oligomeric behavior needed to perform the wide range of functions occurring during the AAV life cycle.
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