ArticleThe Journal of biological chemistry2008
A stromal pool of TatA promotes Tat-dependent protein transport across the thylakoid membrane.
Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
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Who cites it
10 citing papers in PubMed, 29 citations in OpenAlex.
- The mechanism of Tat-dependent protein translocation.Microbial cell (Graz, Austria) · 2026Article
- Length matters: Functional flip of the short TatA transmembrane helix.Biophysical journal · 2023Article
- Isolation of Physiologically Active Thylakoids and Their Use in Energy-Dependent Protein Transport Assays.Journal of visualized experiments : JoVE · 2018Article
- How to achieve Tat transport with alien TatA.Scientific reports · 2017Article
- TatBC-independent TatA/Tat substrate interactions contribute to transport efficiency.PloS one · 2015Article
- The chloroplast twin arginine transport (Tat) component, Tha4, undergoes conformational changes leading to Tat protein transport.The Journal of biological chemistry · 2012Article
- Stoichiometry for binding and transport by the twin arginine translocation system.The Journal of cell biology · 2012Article
- Twin-arginine-dependent translocation of folded proteins.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2012Review
- Transmembrane insertion of twin-arginine signal peptides is driven by TatC and regulated by TatB.Nature communications · 2012Article
- TatB functions as an oligomeric binding site for folded Tat precursor proteins.Molecular biology of the cell · 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
In chloroplasts and bacteria, the Tat (twin-arginine translocation) system is engaged in transporting folded passenger proteins across the thylakoid and cytoplasmic membranes, respectively. To date, three membrane proteins (TatA, TatB, and TatC) have been identified to be essential for Tat-dependent protein translocation in the plant system, whereas soluble factors seem not to be required. In contrast, in the bacterial system, several cytosolic chaperones were described to be involved in Tat transport processes. Therefore, we have examined whether stromal or peripherally associated membrane proteins also play a role in Tat transport across the thylakoid membrane. Analyzing both authentic precursors as well as the chimeric 16/23 protein, which allows us to study each step of the translocation process individually, we demonstrate that a soluble form of TatA is present in the chloroplast stroma, which significantly improves the efficiency of Tat-dependent protein transport. Furthermore, this soluble TatA is able to reconstitute the Tat transport properties of thylakoid membranes that are transport-incompetent due to extraction with solutions of chaotropic salts.
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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.