ArticleBiophysical journal2007
The chloroplast Tat pathway utilizes the transmembrane electric potential as an energy source.
Article in Biophysical journal, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 70 citations in OpenAlex.
- Tat-dependent protein translocation and its evolution.FEMS microbiology reviews · 2026Review
- The mechanism of Tat-dependent protein translocation.Microbial cell (Graz, Austria) · 2026Article
- New insights into the Tat protein transport cycle from characterizing the assembled Tat translocon.Molecular microbiology · 2022Article
- Oligomerization state of the functional bacterial twin-arginine translocation (Tat) receptor complex.Communications biology · 2022Article
- Influence of the TorD signal peptide chaperone on Tat-dependent protein translocation.PloS one · 2021Article
- Transport of Folded Proteins by the Tat System.The protein journal · 2019Review
- The Twin-Arginine Pathway for Protein Secretion.EcoSal Plus · 2019Review
- Routing of thylakoid lumen proteins by the chloroplast twin arginine transport pathway.Photosynthesis research · 2018Review
- Peculiar features of the plastids of the colourless alga Euglena longa and photosynthetic euglenophytes unveiled by transcriptome analyses.Scientific reports · 2018Article
- Thylakoid-integrated recombinant Hcf106 participates in the chloroplast twin arginine transport system.Plant direct · 2018Article
- The Tat protein transport system: intriguing questions and conundrums.FEMS microbiology letters · 2018Review
- A Hinged Signal Peptide Hairpin Enables Tat-Dependent Protein Translocation.Biophysical journal · 2017Article
- How to achieve Tat transport with alien TatA.Scientific reports · 2017Article
- The Role of Light-Dark Regulation of the Chloroplast ATP Synthase.Frontiers in plant science · 2017Article
- Effects of far-red light on fluorescence induction in infiltrated pea leaves under diminished ΔpH and Δφ components of the proton motive force.Journal of bioenergetics and biomembranes · 2013Article
- Intra-plastid protein trafficking: how plant cells adapted prokaryotic mechanisms to the eukaryotic condition.Biochimica et biophysica acta · 2013Review
- Energetic cost of protein import across the envelope membranes of chloroplasts.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Twin-arginine-dependent translocation of folded proteins.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2012Review
- Kinetics of precursor interactions with the bacterial Tat translocase detected by real-time FRET.The Journal of biological chemistry · 2012Article
- Keep the balloon deflated: the significance of protein maturation for thylakoid flattening.Plant signaling & behavior · 2010Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The thylakoid membrane, located inside the chloroplast, requires proteins transported across it for plastid biogenesis and functional photosynthetic electron transport. The chloroplast Tat translocator found on thylakoids transports proteins from the plastid stroma to the thylakoid lumen. Previous studies have shown that the chloroplast Tat pathway is independent of NTP hydrolysis as an energy source and instead depends on the thylakoid transmembrane proton gradient to power protein translocation. Because of its localization on the same membrane as the proton motive force-dependent F(0)F(1) ATPase, we believed that the chloroplast Tat pathway also made use of the thylakoid electric potential for transporting substrates. By adjusting the rate of photosynthetic proton pumping and by utilizing ionophores, we show that the chloroplast Tat pathway can also utilize the transmembrane electric potential for protein transport. Our findings indicate that the chloroplast Tat pathway is likely dependent on the total protonmotive force (PMF) as an energy source. As a protonmotive-dependent device, certain predictions can be made about structural features expected to be found in the Tat translocon, specifically, the presence of a proton well, a device in the membrane that converts electrical potential into chemical potential.
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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.