ArticleNucleic acids research2016
Exclusion of small terminase mediated DNA threading models for genome packaging in bacteriophage T4.
Article in Nucleic acids research, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 20 citations in OpenAlex.
- Treatment ofViruses · 2025Article
- Structural basis for DNA recognition by a viral genome-packaging machine.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Review
- Viral Small Terminase: A Divergent Structural Framework for a Conserved Biological Function.Viruses · 2022Review
- Article
- Biophysical analysis of Pseudomonas-phage PaP3 small terminase suggests a mechanism for sequence-specific DNA-binding by lateral interdigitation.Nucleic acids research · 2020Article
- A thermophilic phage uses a small terminase protein with a fixed helix-turn-helix geometry.The Journal of biological chemistry · 2020Article
- Identification of the First Gene Transfer Agent (GTA) Small Terminase inJournal of virology · 2019Article
- Bacteriophage T4 capsid as a nanocarrier for Peptide-N-Glycosidase F immobilization through self-assembly.Scientific reports · 2019Article
- Packaging of Dinoroseobacter shibae DNA into Gene Transfer Agent Particles Is Not Random.Genome biology and evolution · 2018Article
- Physical and Functional Characterization of a Viral Genome Maturation Complex.Biophysical journal · 2017Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
Abstract
Tailed bacteriophages and herpes viruses use powerful molecular machines to package their genomes. The packaging machine consists of three components: portal, motor (large terminase; TerL) and regulator (small terminase; TerS). Portal, a dodecamer, and motor, a pentamer, form two concentric rings at the special five-fold vertex of the icosahedral capsid. Powered by ATPase, the motor ratchets DNA into the capsid through the portal channel. TerS is essential for packaging, particularly for genome recognition, but its mechanism is unknown and controversial. Structures of gear-shaped TerS rings inspired models that invoke DNA threading through the central channel. Here, we report that mutations of basic residues that line phage T4 TerS (gp16) channel do not disrupt DNA binding. Even deletion of the entire channel helix retained DNA binding and produced progeny phage in vivo On the other hand, large oligomers of TerS (11-mers/12-mers), but not small oligomers (trimers to hexamers), bind DNA. These results suggest that TerS oligomerization creates a large outer surface, which, but not the interior of the channel, is critical for function, probably to wrap viral genome around the ring during packaging initiation. Hence, models involving TerS-mediated DNA threading may be excluded as an essential mechanism for viral genome packaging.
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Registered trials
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