ArticleJournal of virology2001
Minute virus of mice initiator protein NS1 and a host KDWK family transcription factor must form a precise ternary complex with origin DNA for nicking to occur.
Article in Journal of virology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
What it found
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Who cites it
21 citing papers in PubMed, 39 citations in OpenAlex.
- Canine Parvovirus and Its Non-Structural Gene 1 as Oncolytic Agents: Mechanism of Action and Induction of Anti-Tumor Immune Response.Frontiers in oncology · 2021Review
- The NS1 protein of the parvovirus MVM Aids in the localization of the viral genome to cellular sites of DNA damage.PLoS pathogens · 2020Article
- A study on endonuclease BspD6I and its stimulus-responsive switching by modified oligonucleotides.PloS one · 2018Article
- Phosphorylated STAT5 directly facilitates parvovirus B19 DNA replication in human erythroid progenitors through interaction with the MCM complex.PLoS pathogens · 2017Article
- Structures of minute virus of mice replication initiator protein N-terminal domain: Insights into DNA nicking and origin binding.Virology · 2015Article
- The human parvovirus B19 non-structural protein 1 N-terminal domain specifically binds to the origin of replication in the viral DNA.Virology · 2014Article
- Mutations in DNA binding and transactivation domains affect the dynamics of parvovirus NS1 protein.Journal of virology · 2013Article
- Maintenance of the flip sequence orientation of the ears in the parvoviral left-end hairpin is a nonessential consequence of the critical asymmetry in the hairpin stem.Journal of virology · 2012Article
- Parvovirus B19 nonstructural protein-induced damage of cellular DNA and resultant apoptosis.International journal of medical sciences · 2011Article
- Effect of ATP binding and hydrolysis on dynamics of canine parvovirus NS1.Journal of virology · 2010Article
- Article
- A WW-like module in the RAG1 N-terminal domain contributes to previously unidentified protein-protein interactions.Nucleic acids research · 2009Article
- Differential modulation of glucocorticoid and progesterone receptor transactivation.Molecular and cellular endocrinology · 2008Article
- Replication initiator protein NS1 of the parvovirus minute virus of mice binds to modular divergent sites distributed throughout duplex viral DNA.Journal of virology · 2007Article
- Segregation of a single outboard left-end origin is essential for the viability of parvovirus minute virus of mice.Journal of virology · 2006Article
- Reverse genetic system for the analysis of parvovirus telomeres reveals interactions between transcription factor binding sites in the hairpin stem.Journal of virology · 2003Article
- Resolution of parvovirus dimer junctions proceeds through a novel heterocruciform intermediate.Journal of virology · 2003Article
- Regulation of minute virus of mice NS1 replicative functions by atypical PKClambda in vivo.Journal of virology · 2003Article
- Evolutionary dynamics of viral attenuation.Journal of virology · 2002Article
- Parvovirus initiator protein NS1 and RPA coordinate replication fork progression in a reconstituted DNA replication system.Journal of virology · 2002Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
Abstract
Parvoviral rolling hairpin replication generates palindromic genomic concatemers whose junctions are resolved to give unit-length genomes by a process involving DNA replication initiated at origins derived from each viral telomere. The left-end origin of minute virus of mice (MVM), oriL, contains binding sites for the viral initiator nickase, NS1, and parvovirus initiation factor (PIF), a member of the emerging KDWK family of transcription factors. oriL is generated as an active form, oriL(TC), and as an inactive form, oriL(GAA), which contains a single additional nucleotide inserted between the NS1 and PIF sites. Here we examined the interactions on oriL(TC) which lead to activation of NS1 by PIF. The two subunits of PIF, p79 and p96, cooperatively bind two ACGT half-sites, which can be flexibly spaced. When coexpressed from recombinant baculoviruses, the PIF subunits preferentially form heterodimers which, in the presence of ATP, show cooperative binding with NS1 on oriL, but this interaction is preferentially enhanced on oriL(TC) compared to oriL(GAA). Without ATP, NS1 is unable to bind stably to its cognate site, but PIF facilitates this interaction, rendering the NS1 binding site, but not the nick site, resistant to DNase I. Varying the spacing of the PIF half-sites shows that the distance between the NS1 binding site and the NS1-proximal half-site is critical for nickase activation, whereas the position of the distal half-site is unimportant. When expressed separately, both PIF subunits form homodimers that bind site specifically to oriL, but only complexes containing p79 activate the NS1 nickase function.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the Socratic graph.