ArticleThe Journal of biological chemistry2012
The Tat system for membrane translocation of folded proteins recruits the membrane-stabilizing Psp machinery in Escherichia coli.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 24 citations in OpenAlex.
- Essential Role of LapD in the Absence of Cardiolipins.International journal of molecular sciences · 2026Article
- Tat-dependent protein translocation and its evolution.FEMS microbiology reviews · 2026Review
- The mechanism of Tat-dependent protein translocation.Microbial cell (Graz, Austria) · 2026Article
- A larger TatBC complex associates with TatA clusters for transport of folded proteins across the bacterial cytoplasmic membrane.Scientific reports · 2024Article
- Envelope Stress Activates Expression of the Twin Arginine Translocation (Tat) System in Salmonella.Microbiology spectrum · 2022Article
- A Potential Late Stage Intermediate of Twin-Arginine Dependent Protein Translocation inFrontiers in microbiology · 2019Article
- The TatA component of the twin-arginine translocation system locally weakens the cytoplasmic membrane ofThe Journal of biological chemistry · 2018Article
- Evidence for an Adaptation of a Phage-Derived Holin/Endolysin System to Toxin Transport inFrontiers in microbiology · 2018Article
- Evidence for a second regulatory binding site on PspF that is occupied by the C-terminal domain of PspA.PloS one · 2018Article
- Mechanisms of drug resistance: daptomycin resistance.Annals of the New York Academy of Sciences · 2015Review
- Comparative Analysis of Apicoplast-Targeted Protein Extension Lengths in Apicomplexan Parasites.BioMed research international · 2015Article
- TatBC-independent TatA/Tat substrate interactions contribute to transport efficiency.PloS one · 2015Article
- A role of VIPP1 as a dynamic structure within thylakoid centers as sites of photosystem biogenesis?Plant signaling & behavior · 2013Article
- Substrate-dependent assembly of the Tat translocase as observed in live Escherichia coli cells.PloS one · 2013Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Tat systems transport folded proteins across energized membranes of bacteria, archaea, and plant plastids. In Escherichia coli, TatBC complexes recognize the transported proteins, and TatA complexes are recruited to facilitate transport. We achieved an abstraction of TatA from membranes without use of detergents and observed a co-purification of PspA, a membrane-stress response protein. The N-terminal transmembrane domain of TatA was required for the interaction. Electron microscopy displayed TatA complexes in direct contact with PspA. PspB and PspC were important for the TatA-PspA contact. The activator protein PspF was not involved in the PspA-TatA interaction, demonstrating that basal levels of PspA already interact with TatA. Elevated TatA levels caused membrane stress that induced a strictly PspBC- and PspF-dependent up-regulation of PspA. TatA complexes were found to destabilize membranes under these conditions. At native TatA levels, PspA deficiency clearly affected anaerobic TMAO respiratory growth, suggesting that energetic costs for transport of large Tat substrates such as TMAO reductase can become growth limiting in the absence of PspA. The physiological role of PspA recruitment to TatA may therefore be the control of membrane stress at active translocons.
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