ArticleJournal of molecular biology2008
DNA packaging motor assembly intermediate of bacteriophage phi29.
Article in Journal of molecular biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
What it found
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
31 citing papers in PubMed, 42 citations in OpenAlex.
- The Bacteriophage VMY 22 Has Enhanced the Stability of Its Functional Proteins via Adaptive Evolution in a Temperature-Varying Environment.Bioengineering (Basel, Switzerland) · 2026Article
- DNA/RNA hybrids avoid channel gating that leads to the continued packaging of numerous hybrids into the phi29 protein shell.Nucleic acids research · 2025Article
- The LSmAD Domain of Ataxin-2 Modulates the Structure and RNA Binding of Its Preceding LSm Domain.Cells · 2025Article
- Viral Genomic DNA Packaging Machinery.Sub-cellular biochemistry · 2024Review
- Insights into a viral motor: the structure of the HK97 packaging termination assembly.Nucleic acids research · 2023Article
- Revolving hexameric ATPases as asymmetric motors to translocate double-stranded DNA genome along one strand.iScience · 2023Review
- Kinetics of ATP/ADP binding to the gp16 ATPase.Biophysical journal · 2022Article
- Atomistic basis of force generation, translocation, and coordination in a viral genome packaging motor.Nucleic acids research · 2021Article
- A viral genome packaging motor transitions between cyclic and helical symmetry to translocate dsDNA.Science advances · 2021Article
- Article
- NMR structure of a vestigial nuclease provides insight into the evolution of functional transitions in viral dsDNA packaging motors.Nucleic acids research · 2020Article
- ATP/ADP modulates gp16-pRNA conformational change in the Phi29 DNA packaging motor.Nucleic acids research · 2019Article
- Structural assembly of the tailed bacteriophage ϕ29.Nature communications · 2019Article
- Prohead RNA: a noncoding viral RNA of novel structure and function.Wiley interdisciplinary reviews. RNA · 2016Review
- Article
- An RNA Domain Imparts Specificity and Selectivity to a Viral DNA Packaging Motor.Journal of virology · 2015Article
- Adenoviral L4 33K forms ring-like oligomers and stimulates ATPase activity of IVa2: implications in viral genome packaging.Frontiers in microbiology · 2015Article
- The ATPase of the phi29 DNA packaging motor is a member of the hexameric AAA+ superfamily.Virology · 2013Article
- Revolution rather than rotation of AAA+ hexameric phi29 nanomotor for viral dsDNA packaging without coiling.Virology · 2013Article
- Archaeal viruses, not archaeal phages: an archaeological dig.Archaea (Vancouver, B.C.) · 2013Review
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
Abstract
Unraveling the structure and assembly of the DNA packaging ATPases of the tailed double-stranded DNA bacteriophages is integral to understanding the mechanism of DNA translocation. Here, the bacteriophage phi29 packaging ATPase gene product 16 (gp16) was overexpressed in soluble form in Bacillus subtilis (pSAC), purified to near homogeneity, and assembled to the phi29 precursor capsid (prohead) to produce a packaging motor intermediate that was fully active in in vitro DNA packaging. The formation of higher oligomers of the gp16 from monomers was concentration dependent and was characterized by analytical ultracentrifugation, gel filtration, and electron microscopy. The binding of multiple copies of gp16 to the prohead was dependent on the presence of an oligomer of 174- or 120-base prohead RNA (pRNA) fixed to the head-tail connector at the unique portal vertex of the prohead. The use of mutant pRNAs demonstrated that gp16 bound specifically to the A-helix of pRNA, and ribonuclease footprinting of gp16 on pRNA showed that gp16 protected the CC residues of the CCA bulge (residues 18-20) of the A-helix. The binding of gp16 to the prohead/pRNA to constitute the complete and active packaging motor was confirmed by cryo-electron microscopy three-dimensional reconstruction of the prohead/pRNA/gp16 complex. The complex was capable of supercoiling DNA-gp3 as observed previously for gp16 alone; therefore, the binding of gp16 to the prohead, rather than first to DNA-gp3, represents an alternative packaging motor assembly pathway.
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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 OpenQuestion graph.