Details
| Original language | English |
|---|---|
| Pages (from-to) | 507-523 |
| Number of pages | 17 |
| Journal | Biomolecular Concepts |
| Volume | 2 |
| Issue number | 6 |
| Publication status | Published - 1 Dec 2011 |
Abstract
The twin-arginine translocation (Tat) pathway is found in bacteria, archaea, and plant chloroplasts, where it is dedicated to the transmembrane transport of fully folded proteins. These proteins contain N-terminal signal peptides with a specific Tat-system binding motif that is recognized by the transport machinery. In contrast to other protein transport systems, the Tat system consists of multiple copies of only two or three usually small (∼8-30 kDa) membrane proteins that oligomerize to two large complexes that transiently interact during translocation. Only one of these complexes includes a polytopic membrane protein, TatC. The other complex consists of TatA. Tat systems of plants, proteobacteria, and several other phyla contain a third component, TatB. TatB is evolutionarily and structurally related to TatA and usually forms tight complexes with TatC. Minimal two-component Tat systems lacking TatB are found in many bacterial and archaeal phyla. They consist of a 'bifunctional' TatA that also covers TatB functionalities, and a TatC. Recent insights into the structure and interactions of the Tat proteins have various important implications.
Keywords
- protein folding, protein transport, redox protein biogenesis, twin-arginine translocation
ASJC Scopus subject areas
Cite this
- Standard
- Harvard
- Apa
- Vancouver
- BibTeX
- RIS
In: Biomolecular Concepts, Vol. 2, No. 6, 01.12.2011, p. 507-523.
Research output: Contribution to journal › Review article › Research › peer review
}
TY - JOUR
T1 - The Tat-dependent protein translocation pathway
AU - Hou, Bou
AU - Brüser, Thomas
N1 - Funding Information: Support by the Deutsche Forschungsgemeinschaft (grant BR2285/ 1-3) is gratefully acknowledged. Publisher Copyright: © 2011 by Walter de Gruyter Berlin Boston 2011. Copyright: Copyright 2015 Elsevier B.V., All rights reserved.
PY - 2011/12/1
Y1 - 2011/12/1
N2 - The twin-arginine translocation (Tat) pathway is found in bacteria, archaea, and plant chloroplasts, where it is dedicated to the transmembrane transport of fully folded proteins. These proteins contain N-terminal signal peptides with a specific Tat-system binding motif that is recognized by the transport machinery. In contrast to other protein transport systems, the Tat system consists of multiple copies of only two or three usually small (∼8-30 kDa) membrane proteins that oligomerize to two large complexes that transiently interact during translocation. Only one of these complexes includes a polytopic membrane protein, TatC. The other complex consists of TatA. Tat systems of plants, proteobacteria, and several other phyla contain a third component, TatB. TatB is evolutionarily and structurally related to TatA and usually forms tight complexes with TatC. Minimal two-component Tat systems lacking TatB are found in many bacterial and archaeal phyla. They consist of a 'bifunctional' TatA that also covers TatB functionalities, and a TatC. Recent insights into the structure and interactions of the Tat proteins have various important implications.
AB - The twin-arginine translocation (Tat) pathway is found in bacteria, archaea, and plant chloroplasts, where it is dedicated to the transmembrane transport of fully folded proteins. These proteins contain N-terminal signal peptides with a specific Tat-system binding motif that is recognized by the transport machinery. In contrast to other protein transport systems, the Tat system consists of multiple copies of only two or three usually small (∼8-30 kDa) membrane proteins that oligomerize to two large complexes that transiently interact during translocation. Only one of these complexes includes a polytopic membrane protein, TatC. The other complex consists of TatA. Tat systems of plants, proteobacteria, and several other phyla contain a third component, TatB. TatB is evolutionarily and structurally related to TatA and usually forms tight complexes with TatC. Minimal two-component Tat systems lacking TatB are found in many bacterial and archaeal phyla. They consist of a 'bifunctional' TatA that also covers TatB functionalities, and a TatC. Recent insights into the structure and interactions of the Tat proteins have various important implications.
KW - protein folding
KW - protein transport
KW - redox protein biogenesis
KW - twin-arginine translocation
UR - http://www.scopus.com/inward/record.url?scp=84865007676&partnerID=8YFLogxK
U2 - 10.1515/BMC.2011.040
DO - 10.1515/BMC.2011.040
M3 - Review article
AN - SCOPUS:84865007676
VL - 2
SP - 507
EP - 523
JO - Biomolecular Concepts
JF - Biomolecular Concepts
SN - 1868-5021
IS - 6
ER -