ArticleJournal of virology2012
Membrane interaction of the portal protein gp20 of bacteriophage T4.
Article in Journal of virology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
9 citing papers in PubMed.
- Engineering ofCells · 2023Article
- Review
- Review
- The remarkable viral portal vertex: structure and a plausible model for mechanism.Current opinion in virology · 2021Review
- The multi-drug efflux system AcrABZ-TolC is essential for infection ofJournal of virology · 2021Article
- Capsids and Portals Influence Each Other's Conformation During Assembly and Maturation.Journal of molecular biology · 2020Article
- Three-step channel conformational changes common to DNA packaging motors of bacterial viruses T3, T4, SPP1, and Phi29.Virology · 2017Article
- Cryo-EM structure of the bacteriophage T4 portal protein assembly at near-atomic resolution.Nature communications · 2015Article
- Structure-function analysis of the DNA translocating portal of the bacteriophage T4 packaging machine.Journal of molecular biology · 2014Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Assembly of the bacteriophage T4 head structure occurs at the cytoplasmic face of the inner membrane of Escherichia coli with the formation of proheads. The proheads contain an internal scaffolding core that determines the size and the structure of the capsid. In a mutant where the major shell protein gp23 was compromised, core structures without a shell had been detected. Such core structures were also found in the mutant T4am20am23. Since the mutation in gene 20 is at the N terminus of gp20, it was assumed that these core structures assemble in the absence of gp20. However, sequencing showed that the mutation introduces a new ribosome binding site that leads to a restart at codon 15. Although the mutant protein gp20s lacks the very N-terminal sequence, we found that it still binds to the membrane of the host cell and can initiate prohead assembly. This explains its activity to allow the assembly of core structures and proheads at the membrane surface. With a cross-linking approach, we show here that gp20 and gp20s are escorted by the chaperones DnaK, trigger factor, and GroEL and dock on the membrane at the membrane protein YidC.
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Registered trials
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