ArticlePloS one2021
Selective transport of fluorescent proteins into the phage nucleus.
Article in PloS one, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 27 citations in OpenAlex.
- The biology of jumbo phages.Nature communications · 2026Review
- The phage nucleus synergizes with an anti-defense protein to resist bacterial immunity.Cell reports · 2026Article
- The complex developmental mechanisms of nucleus-forming jumbo phages.Current opinion in microbiology · 2025Review
- Unexplored diversity and molecular genetic signatures of chimallin and phuz encoding phages.BMC genomics · 2025Article
- The Biology of Nucleus-Forming Jumbo Phages.Annual review of genetics · 2025Review
- Sequential membrane- and protein-bound organelles compartmentalize genomes during phage infection.Cell host & microbe · 2025Article
- CRISPRi-ART enables functional genomics of diverse bacteriophages using RNA-binding dCas13d.Nature microbiology · 2025Article
- Erwinia phage Asesino is a nucleus-forming phage that lacks PhuZ.Scientific reports · 2025Article
- Genomic transfer via membrane vesicle: a strategy of giant phage phiKZ for early infection.Journal of virology · 2024Article
- A transcriptionally active lipid vesicle encloses the injectedbioRxiv : the preprint server for biology · 2024Article
- An intron endonuclease facilitates interference competition between coinfecting viruses.Science (New York, N.Y.) · 2024Article
- The intricate organizational strategy of nucleus-forming phages.Current opinion in microbiology · 2024Review
- Nucleus-forming jumbophage PhiKZ therapeutically outcompetes non-nucleus-forming jumbophage Callisto.iScience · 2024Article
- Asesino: a nucleus-forming phage that lacks PhuZ.bioRxiv : the preprint server for biology · 2024Article
- An essential and highly selective protein import pathway encoded by nucleus-forming phage.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Jumbo phages are active against extensively drug-resistant eyedrop-associatedAntimicrobial agents and chemotherapy · 2023Article
- Identification of the bacteriophage nucleus protein interaction network.Nature structural & molecular biology · 2023Article
- Identifying the core genome of the nucleus-forming bacteriophage family and characterization of Erwinia phage RAY.Cell reports · 2023Article
- Identification of the bacteriophage nucleus protein interaction network.bioRxiv : the preprint server for biology · 2023Article
- Structural studies of the nucleus-like assembly of jumbo bacteriophage 201φ2-1.Frontiers in microbiology · 2023Article
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Authors and funding
9 authors at 1 institution in 1 country.
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Abstract
Upon infection of Pseudomonas cells, jumbo phages 201Φ2-1, ΦPA3, and ΦKZ assemble a phage nucleus. Viral DNA is enclosed within the phage-encoded proteinaceous shell along with proteins associated with DNA replication, recombination and transcription. Ribosomes and proteins involved in metabolic processes are excluded from the nucleus. RNA synthesis occurs inside the phage nucleus and messenger RNA is presumably transported into the cytoplasm to be translated. Newly synthesized proteins either remain in the cytoplasm or specifically translocate into the nucleus. The molecular mechanisms governing selective protein sorting and nuclear import in these phage infection systems are currently unclear. To gain insight into this process, we studied the localization of five reporter fluorescent proteins (GFP+, sfGFP, GFPmut1, mCherry, CFP). During infection with ΦPA3 or 201Φ2-1, all five fluorescent proteins were excluded from the nucleus as expected; however, we have discovered an anomaly with the ΦKZ nuclear transport system. The fluorescent protein GFPmut1, expressed by itself, was transported into the ΦKZ phage nucleus. We identified the amino acid residues on the surface of GFPmut1 required for nuclear targeting. Fusing GFPmut1 to any protein, including proteins that normally reside in the cytoplasm, resulted in transport of the fusion into the nucleus. Although the mechanism of transport is still unknown, we demonstrate that GFPmut1 is a useful tool that can be used for fluorescent labelling and targeting of proteins into the ΦKZ phage nucleus.
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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.