ArticleThe Journal of biological chemistry2011
Dynamics of the T4 bacteriophage DNA packasome motor: endonuclease VII resolvase release of arrested Y-DNA substrates.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 29 citations in OpenAlex.
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- Efficient synthesis of CRISPR-Cas13a-antimicrobial capsids against MRSA facilitated by silent mutation incorporation.Scientific reports · 2024Article
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- Mechanism of Viral DNA Packaging in Phage T4 Using Single-Molecule Fluorescence Approaches.Viruses · 2024Review
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- Tryptophan Residues Are Critical for Portal Protein Assembly and Incorporation in Bacteriophage P22.Viruses · 2022Article
- The T4 TerL Prohead Packaging Motor Does Not Drive DNA Translocation by a Proposed Dehydration Mechanism.Viruses · 2020Article
- Concurrent Exposure of Neutralizing and Non-neutralizing Epitopes on a Single HIV-1 Envelope Structure.Frontiers in immunology · 2019Article
- The large terminase DNA packaging motor grips DNA with its ATPase domain for cleavage by the flexible nuclease domain.Nucleic acids research · 2017Article
- DNA Scrunching in the Packaging of Viral Genomes.The journal of physical chemistry. B · 2016Article
- Proteomic Analysis of a Novel Bacillus Jumbo Phage Revealing Glycoside Hydrolase As Structural Component.Frontiers in microbiology · 2016Article
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- Review
- Viral nanoparticle-encapsidated enzyme and restructured DNA for cell delivery and gene expression.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Structure-function analysis of the DNA translocating portal of the bacteriophage T4 packaging machine.Journal of molecular biology · 2014Article
- The C-terminal domain of the bacteriophage T4 terminase docks on the prohead portal clip region during DNA packaging.Virology · 2013Article
- Compression of the DNA substrate by a viral packaging motor is supported by removal of intercalating dye during translocation.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- The dynamic pause-unpackaging state, an off-translocation recovery state of a DNA packaging motor from bacteriophage T4.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Dualities in the analysis of phage DNA packaging motors.Bacteriophage · 2012Article
- Portal-large terminase interactions of the bacteriophage T4 DNA packaging machine implicate a molecular lever mechanism for coupling ATPase to DNA translocation.Journal of virology · 2012Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Conserved bacteriophage ATP-based DNA translocation motors consist of a multimeric packaging terminase docked onto a unique procapsid vertex containing a portal ring. DNA is translocated into the empty procapsid through the portal ring channel to high density. In vivo the T4 phage packaging motor deals with Y- or X-structures in the replicative concatemer substrate by employing a portal-bound Holliday junction resolvase that trims and releases these DNA roadblocks to packaging. Here using dye-labeled packaging anchored 3.7-kb Y-DNAs or linear DNAs, we demonstrate FRET between the dye-labeled substrates and GFP portal-containing procapsids and between GFP portal and single dye-labeled terminases. We show using FRET-fluorescence correlation spectroscopy that purified T4 gp49 endonuclease VII resolvase can release DNA compression in vitro in prohead portal packaging motor anchored and arrested Y-DNA substrates. In addition, using active terminases labeled at the N- and C-terminal ends with a single dye molecule, we show by FRET distance of the N-terminal GFP-labeled portal protein containing prohead at 6.9 nm from the N terminus and at 5.7 nm from the C terminus of the terminase. Packaging with a C-terminal fluorescent terminase on a GFP portal prohead, FRET shows a reduction in distance to the GFP portal of 0.6 nm in the arrested Y-DNA as compared with linear DNA; the reduction is reversed by resolvase treatment. Conformational changes in both the motor proteins and the DNA substrate itself that are associated with the power stroke of the motor are consistent with a proposed linear motor employing a terminal-to-portal DNA grip-and-release mechanism.
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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.