ArticleEMBO reports2023
A glycine zipper motif is required for the translocation of a T6SS toxic effector into target cells.
Article in EMBO reports, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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Who cites it
8 citing papers in PubMed, 13 citations in OpenAlex.
- Review
- Salt bridge disruption in colicin Ib channel-forming domain enhances membrane translocation and bactericidal activity.Journal of structural biology: X · 2026Article
- A toxic effector of T7SS facilitates bacterial competition and virulence through membrane damage in Streptococcus suis.Veterinary research · 2026Article
- Not just passengers: effectors contribute to the assembly of the type VI secretion system as structural building blocks.Journal of bacteriology · 2025Review
- Differential expression of theApplied and environmental microbiology · 2024Article
- Identification of type VI secretion system effector-immunity pairs using structural bioinformatics.Molecular systems biology · 2024Article
- Protein-Protein Interactions: Co-immunoprecipitation.Methods in molecular biology (Clifton, N.J.) · 2024Article
- A glycine zipper motif is required for the translocation of a T6SS toxic effector into target cells.EMBO reports · 2023Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Type VI secretion systems (T6SSs) can deliver diverse toxic effectors into eukaryotic and bacterial cells. Although much is known about the regulation and assembly of T6SS, the translocation mechanism of effectors into the periplasm and/or cytoplasm of target cells remains elusive. Here, we use the Agrobacterium tumefaciens DNase effector Tde1 to unravel the mechanism of translocation from attacker to prey. We demonstrate that Tde1 binds to its adaptor Tap1 through the N-terminus, which harbors continuous copies of GxxxG motifs resembling the glycine zipper structure found in proteins involved in the membrane channel formation. Amino acid substitutions on G
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Registered trials
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