Tat-dependent protein translocation and its evolution

Clicks: 17
ID: 329434
2026
Free PDF
Article Quality & Performance Metrics
Overall Quality
Not rated
Combines reader engagement with the AI quality analysis. This article has not been analysed, so there is no overall score — reader engagement is measured and shown alongside.
AI Quality Assessment
Not analyzed
Readership in this journal
Emerging

Ranked #50 of 108 articles by views in FEMS microbiology reviews

Most read Least read

Bar heights use a square-root scale.

Mint this article as an NFT
Not yet minted

Create a permanent, verifiable on-chain record of this article on the Scimatic Network. The NFT is held in your Journament account, and you can withdraw it to your own wallet at any time.

5 SUSD one-off · no wallet required
Sign in to mint
Abstract
The Tat system is a general translocation machinery responsible for the transport of folded proteins across biological membranes that are energized by a proton or sodium motive force at these membranes. Protein substrates are characterized by usually amino-terminal signal peptides harboring a conserved twin-arginine sequence motif. Phylogenetic analyses suggest that a Tat system was already present in the last universal common ancestor (LUCA). Today, Tat systems are found in bacteria, archaea, and bacteria-derived organelles. Minimally, Tat systems are composed of one TatC-family component and one TatA/B-family component, with multiple copies of these components forming the functional translocon, while more complex Tat systems exist that require additional homologs of TatA/B or TatC. Due to its ability to translocate folded proteins with bound cofactors, the Tat system is essential for a wide range of important physiological pathways, such as many anaerobic respirations or photosynthesis. With a focus on evolutionary aspects, and by including recent structural and mechanistic insights, we herein review our current knowledge on this mechanistically unique translocation pathway.
Reference Key
openalex_W7167015089 Use this key to autocite in the manuscript while using SciMatic Manuscript Manager or Thesis Manager
Authors Thomas Brüser, Carsten Sanders
Journal FEMS microbiology reviews
Year 2026
DOI
10.1093/femsre/fuag052
URL
https://doi.org/10.1093/femsre/fuag052
Keywords Keywords not found

Citations

No citations found. To add a citation, contact the admin at info@scimatic.org

Comments

No comments yet. Be the first to comment on this article.