ArticleJournal of molecular biology2013
Functional domains of the HK97 capsid maturation protease and the mechanisms of protein encapsidation.
Article in Journal of molecular biology, 2013. 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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Who cites it
27 citing papers in PubMed, 38 citations in OpenAlex.
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- Use of an Integrated Approach Involving AlphaFold Predictions for the Evolutionary Taxonomy ofBiomolecules · 2023Article
- Genome Sequences and Characteristics of Six Cluster B1 Mycobacteriophages Discovered at Saint Joseph's University.Microbiology resource announcements · 2022Article
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- A Cut above the Rest: Characterization of the Assembly of a Large Viral Icosahedral Capsid.Viruses · 2020Article
- Phage G Structure at 6.1 Å Resolution, Condensed DNA, and Host Identity Revision to a Lysinibacillus.Journal of molecular biology · 2020Article
- Capsids and Portals Influence Each Other's Conformation During Assembly and Maturation.Journal of molecular biology · 2020Article
- Structural assembly of the tailed bacteriophage ϕ29.Nature communications · 2019Article
- Nanoreactor Design Based on Self-Assembling Protein Nanocages.International journal of molecular sciences · 2019Review
- A Hyperthermophilic Phage Decoration Protein Suggests Common Evolutionary Origin with Herpesvirus Triplex Proteins and an Anti-CRISPR Protein.Structure (London, England : 1993) · 2018Article
- Roger Hendrix: Gentle Provocateur.Journal of bacteriology · 2018Review
- Correct Assembly of the Bacteriophage T5 Procapsid Requires Both the Maturation Protease and the Portal Complex.Journal of molecular biology · 2016Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Tailed double-stranded DNA bacteriophages and herpesviruses build capsids by co-assembling a major capsid protein with an internal scaffolding protein that then exits from the assembled structure either intact or after digestion in situ by a protease. In bacteriophage HK97, the 102-residue N-terminal delta domain of the major capsid protein is also removed by proteolysis after assembly and appears to perform the scaffolding function. We describe the HK97 protease that carries out these maturation cleavages. Insertion mutations at seven sites in the protease gene produced mutant proteins that assemble into proheads, and those in the N-terminal two-thirds were enzymatically inactive. Plasmid-expressed protease was rapidly cleaved in vivo but was stabilized by co-expression with the delta domain. Purified protease was found to be active during the assembly of proheads in vitro. Heterologous fusions to the intact protease or to C-terminal fragments targeted fusion proteins into proheads. We confirm that the catalytic activity resides in the N-terminal two-thirds of the protease polypeptide and suggest that the C-terminal one-fifth of the protein contains a capsid targeting signal. The implications of this arrangement are compared to capsid targeting systems in other phages, herpesviruses, and encapsulins.
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Registered trials
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