ArticleThe Journal of biological chemistry2018
The early mature part of bacterial twin-arginine translocation (Tat) precursor proteins contributes to TatBC receptor binding.
Article in The Journal of biological chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 11 citations in OpenAlex.
- Tat-dependent protein translocation and its evolution.FEMS microbiology reviews · 2026Review
- Synergistic Engineering of the Twin-Arginine Translocation (Tat) Pathway and Membrane Capacity Enhances Extracellular Production of Amylosucrase inMicroorganisms · 2025Article
- Analysis of the Brucella suis Twin Arginine Translocation System and Its Substrates Shows That It Is Essential for Viability.Infection and immunity · 2023Article
- Twin-arginine translocase component TatB performs folding quality control via a chaperone-like activity.Scientific reports · 2022Article
- Targeting of proteins to the twin-arginine translocation pathway.Molecular microbiology · 2020Review
- Surface-exposed domains of TatB involved in the structural and functional assembly of the Tat translocase inThe Journal of biological chemistry · 2019Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The twin-arginine translocation (Tat) pathway transports folded proteins across bacterial membranes. Tat precursor proteins possess a conserved twin-arginine (RR) motif in their signal peptides that is involved in the binding of the proteins to the membrane-associated TatBC receptor complex. In addition, the hydrophobic region in the Tat signal peptides also contributes to TatBC binding, but whether regions beyond the signal-peptide cleavage site are involved in this process is unknown. Here, we analyzed the contribution of the early mature protein part of the
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