ArticleMicrobial cell (Graz, Austria)2026
The mechanism of Tat-dependent protein translocation.
Article in Microbial cell (Graz, Austria), 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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Who cites it
2 citing papers in PubMed.
- Identification of the plant mitochondrial OrfX protein: A mass spectrometry approach.FEBS letters · 2026Article
- Tat-dependent protein translocation and its evolution.FEMS microbiology reviews · 2026Review
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2 authors.
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Abstract
The twin-arginine translocation (Tat) system is the only general pathway for the transport of folded proteins across energized biological membranes. It is found in the bacterial or archaeal cytoplasmic membrane, the plant thylakoid membrane or the inner membrane of plant mitochondria. The biological importance of this translocation system can be exemplified by the fact that all bacterial or plant photosynthesis and photosynthetic oxygen evolution on earth requires this system. Despite many biochemical and biophysical studies, the Tat mechanism has been puzzling since the system was discovered in the 1990ies. Important characteristics of the Tat system could not be explained, and also recent high-resolution structures of the Tat system's core with bound substrate has not led to a general transport mechanism yet. In this integrative review, we attempted to answer the key open questions relevant to the Tat mechanism and thereby developed an in its molecular detail new comprehensive explanation of how folded proteins are translocated across membranes by the Tat system.
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