ArticleThe Journal of biological chemistry2013
Regulation of a viral proteinase by a peptide and DNA in one-dimensional space: II. adenovirus proteinase is activated in an unusual one-dimensional biochemical reaction.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 34 citations in OpenAlex.
- Breaking the Chain: Protease Inhibitors as Game Changers in Respiratory Viruses Management.International journal of molecular sciences · 2024Review
- Complex regulation of mitochondrial signaling by human adenovirus minor capsid protein VI.Journal of virology · 2024Article
- Structure of a Cell Entry Defective Human Adenovirus Provides Insights into Precursor Proteins and Capsid Maturation.Journal of molecular biology · 2022Article
- Adenovirus Core Proteins: Structure and Function.Viruses · 2021Review
- Dynamic competition for hexon binding between core protein VII and lytic protein VI promotes adenovirus maturation and entry.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Atomic Structures of Minor Proteins VI and VII in Human Adenovirus.Journal of virology · 2017Article
- Diatrack particle tracking software: Review of applications and performance evaluation.Traffic (Copenhagen, Denmark) · 2017Review
- A Simple, Robust, and High Throughput Single Molecule Flow Stretching Assay Implementation for Studying Transport of Molecules Along DNA.Journal of visualized experiments : JoVE · 2017Article
- Sliding on DNA: From Peptides to Small Molecules.Angewandte Chemie (International ed. in English) · 2016Article
- Molecular sled sequences are common in mammalian proteins.Nucleic acids research · 2016Article
- Molecular sled is an eleven-amino acid vehicle facilitating biochemical interactions via sliding components along DNA.Nature communications · 2016Article
- Speeding up biomolecular interactions by molecular sledding.Chemical science · 2016Article
- Components of Adenovirus Genome Packaging.Frontiers in microbiology · 2016Review
- A Single Maturation Cleavage Site in Adenovirus Impacts Cell Entry and Capsid Assembly.Journal of virology · 2016Article
- Structures of Adenovirus Incomplete Particles Clarify Capsid Architecture and Show Maturation Changes of Packaging Protein L1 52/55k.Journal of virology · 2015Article
- Review
- Structures and organization of adenovirus cement proteins provide insights into the role of capsid maturation in virus entry and infection.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- The cleaved N-terminus of pVI binds peripentonal hexons in mature adenovirus.Journal of molecular biology · 2014Article
- Processing of the l1 52/55k protein by the adenovirus protease: a new substrate and new insights into virion maturation.Journal of virology · 2014Article
- Regulation of a viral proteinase by a peptide and DNA in one-dimensional space: I. binding to DNA AND to hexon of the precursor to protein VI, pVI, of human adenovirus.The Journal of biological chemistry · 2013Article
Corrections and comments
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Authors and funding
9 authors at 4 institutions in 2 countries.
Funding
Abstract
Late in an adenovirus infection, the viral proteinase (AVP) becomes activated to process virion precursor proteins used in virus assembly. AVP is activated by two cofactors, the viral DNA and pVIc, an 11-amino acid peptide originating from the C terminus of the precursor protein pVI. There is a conundrum in the activation of AVP in that AVP and pVI are sequence-independent DNA-binding proteins with nm equilibrium dissociation constants such that in the virus particle, they are predicted to be essentially irreversibly bound to the viral DNA. Here, we resolve that conundrum by showing that activation of AVP takes place on the one-dimensional contour of DNA. In vitro, pVI, a substrate, slides on DNA via one-dimensional diffusion, D(1) = 1.45 × 10(6) bp(2)/s, until it binds to AVP also on the same DNA molecule. AVP, partially activated by being bound to DNA, excises pVIc, which binds to the AVP molecule that cut it out. pVIc then forms a disulfide bond with AVP forming the fully active AVP-pVIc complex bound to DNA. In vivo, in heat-disrupted immature virus, AVP was also activated by pVI in DNA-dependent reactions. This activation mechanism illustrates a new paradigm for virion maturation and a new way, by sliding on DNA, for bimolecular complexes to form among proteins not involved in DNA metabolism.
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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.