ArticleJournal of molecular biology2007
Molecular dissection of ø29 scaffolding protein function in an in vitro assembly system.
Article in Journal of molecular biology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
27 citing papers in PubMed, 44 citations in OpenAlex.
- Phi29 assembly intermediates reveal how scaffold interactions with capsid protein drive capsid construction and maturation.Science advances · 2025Article
- In Vitro Assembly of Virus-Like Particles and Their Applications.Life (Basel, Switzerland) · 2021Review
- Virus capsid assembly across different length scales inspire the development of virus-based biomaterials.Current opinion in virology · 2019Review
- Structural assembly of the tailed bacteriophage ϕ29.Nature communications · 2019Article
- Coat Protein Mutations That Alter the Flux of Morphogenetic Intermediates through the ϕX174 Early Assembly Pathway.Journal of virology · 2017Article
- Article
- ϕX174 Procapsid Assembly: Effects of an Inhibitory External Scaffolding Protein and Resistant Coat Proteins In Vitro.Journal of virology · 2017Article
- Genes essential for the morphogenesis of the Shiga toxin 2-transducing phage from Escherichia coli O157:H7.Scientific reports · 2016Article
- The Minor Capsid Protein VP11 of Thermophilic Bacteriophage P23-77 Facilitates Virus Assembly by Using Lipid-Protein Interactions.Journal of virology · 2015Article
- Electrostatic interactions drive the self-assembly and the transcription activity of the Pseudomonas phage ϕ6 procapsid.Journal of virology · 2014Article
- Highly specific salt bridges govern bacteriophage P22 icosahedral capsid assembly: identification of the site in coat protein responsible for interaction with scaffolding protein.Journal of virology · 2014Article
- Effects of an early conformational switch defect during ϕX174 morphogenesis are belatedly manifested late in the assembly pathway.Journal of virology · 2013Article
- Conformational switch-defective X174 internal scaffolding proteins kinetically trap assembly intermediates before procapsid formation.Journal of virology · 2012Article
- Virus maturation.Annual review of biophysics · 2012Review
- Article
- The bacteriophage lambda gpNu3 scaffolding protein is an intrinsically disordered and biologically functional procapsid assembly catalyst.Journal of molecular biology · 2011Article
- The Staphylococcus aureus pathogenicity island 1 protein gp6 functions as an internal scaffold during capsid size determination.Journal of molecular biology · 2011Article
- A docking model based on mass spectrometric and biochemical data describes phage packaging motor incorporation.Molecular & cellular proteomics : MCP · 2010Article
- P22 coat protein structures reveal a novel mechanism for capsid maturation: stability without auxiliary proteins or chemical crosslinks.Structure (London, England : 1993) · 2010Article
- In vitro incorporation of the phage Phi29 connector complex.Virology · 2009Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
Abstract
An in vitro assembly system was developed to study prolate capsid assembly of phage ø29 biochemically, and to identify regions of scaffolding protein required for its functions. The crowding agent polyethylene glycol can induce bacteriophage ø29 monomeric capsid protein and dimeric scaffolding protein to co-assemble to form particles which have the same geometry as either prolate T=3 Q=5 procapsids formed in vivo or previously observed isometric particles. The formation of particles is a scaffolding-dependent reaction. The balance between the fidelity and efficiency of assembly is controlled by the concentration of crowding agent and temperature. The assembly process is salt sensitive, suggesting that the interactions between the scaffolding and coat proteins are electrostatic. Three N-terminal ø29 scaffolding protein deletion mutants, Delta 1-9, Delta 1-15 and Delta 1-22, abolish the assembly activity. Circular dichroism spectra indicate that these N-terminal deletions are accompanied by a loss of helicity. The inability of these proteins to dimerize suggests that the N-terminal region of the scaffolding protein contributes to the dimer interface and maintains the structural integrity of the dimeric protein. Two C-terminal scaffolding protein deletion mutants, Delta 79-97 and Delta 62-97, also fail to promote assembly. However, the secondary structure and the dimerization ability of these mutants are unchanged relative to wild-type, which suggests that the C terminus is the likely site of interaction with the capsid protein.
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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.