ArticlePloS one2010
Tus, an E. coli protein, contains mammalian nuclear targeting and exporting signals.
Article in PloS one, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 17 citations in OpenAlex.
- Identification of candidate nucleomodulins in ESKAPE bacteria -Frontiers in cellular and infection microbiology · 2026Article
- Engineering and comparison of cas12a-based genome editing systems in plants.The Plant journal : for cell and molecular biology · 2025Article
- Nucleomodulins from gut bacteria: diverse mechanisms of translocation and interaction with host nuclear processes.Applied and environmental microbiology · 2025Review
- Nuclear localization signal-tagged systems: relevant nuclear import principles in the context of current therapeutic design.Chemical Society reviews · 2024Review
- Transgenic mice encoding modern imaging probes: Properties and applications.Cell reports · 2022Review
- Quantitative tracking of protein trafficking to the nucleus using cytosolic protein delivery by nanoparticle-stabilized nanocapsules.Bioconjugate chemistry · 2015Article
- Dynamic localization and the associated translocation mechanism of HMGBs in response to GCRV challenge in CIK cells.Cellular & molecular immunology · 2015Article
- Functional eukaryotic nuclear localization signals are widespread in terminal proteins of bacteriophages.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Shuttling of proteins between nucleus and cytoplasm in mammalian cells is facilitated by the presence of nuclear localization signals (NLS) and nuclear export signals (NES), respectively. However, we have found that Tus, an E. coli replication fork arresting protein, contains separate sequences that function efficiently as NLS and NES in mammalian cell lines, as judged by cellular location of GFP-fusion proteins. The NLS was localized to a short stretch of 9 amino acids in the carboxy-terminus of Tus protein. Alterations of any of these basic amino acids almost completely abolished the nuclear targeting. The NES comprises a cluster of leucine/hydrophobic residues located within 21 amino acids at the amino terminus of Tus. Finally, we have shown that purified GFP-Tus fusion protein or GFP-Tus NLS fusion protein, when added to the culture media, was internalized very efficiently into mammalian cells. Thus, Tus is perhaps the first reported bacterial protein to possess both NLS and NES, and has the capability to transduce protein into mammalian cells.
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Registered trials
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