Details
| Original language | English |
|---|---|
| Pages (from-to) | 7-17 |
| Number of pages | 11 |
| Journal | Microbiological Research |
| Volume | 158 |
| Issue number | 1 |
| Publication status | Published - 2003 |
Abstract
The twin arginine translocation (Tat) system is a machinery which can translocate folded proteins across energy transducing membranes. Currently it is supposed that Tat substrates bind directly to Tat translocon components before a ΔpH-driven translocation occurs. In this review, an alternative model is presented which proposes that membrane integration could precede Tat-dependent translocation. This idea is mainly supported by the recent observations of Tat-independent membrane insertion of Tat substrates in vivo and in vitro. Membrane insertion may allow i) a quality control of the folded state by membrane bound proteases like FtsH, ii) the recognition of the membrane spanning signal peptide by Tat system components, and iii) a pulling mechanism of translocation. In some cases of folded Tat substrates, the membrane targeting process may require ATP-dependent N-terminal unfolding-steps.
ASJC Scopus subject areas
- Immunology and Microbiology(all)
- Microbiology
Cite this
- Standard
- Harvard
- Apa
- Vancouver
- BibTeX
- RIS
In: Microbiological Research, Vol. 158, No. 1, 2003, p. 7-17.
Research output: Contribution to journal › Review article › Research › peer review
}
TY - JOUR
T1 - An alternative model of the twin arginine translocation system
AU - Brüser, Thomas
AU - Sanders, Carsten
N1 - Funding Information: We thank Fevzi Daldal for many challenging discussions and support. We are indebted to Takahiro Yano for manifold input and ideas, especially during the development of the membrane weakening and pulling hypothesis. We are very grateful to Ralf Bernd Klösgen and Bo Hou for cooperation and discussion of each others data prior to publication. Further we would like to thank Tracy Palmer for the donation of strains, Teru Ogura for communication about FtsH and Ute Lech-ner for critically reading this manuscript. We thank especially Jan Remmer Andreesen for his support of this work. C.S. is supported by NIH grant GM38237 to Fevzi Daldal. This work was supported by the grant BMBF-LPD 9901/8-14 of the German Academy of Natural Scientists Leopoldina to T.B. Copyright: Copyright 2017 Elsevier B.V., All rights reserved.
PY - 2003
Y1 - 2003
N2 - The twin arginine translocation (Tat) system is a machinery which can translocate folded proteins across energy transducing membranes. Currently it is supposed that Tat substrates bind directly to Tat translocon components before a ΔpH-driven translocation occurs. In this review, an alternative model is presented which proposes that membrane integration could precede Tat-dependent translocation. This idea is mainly supported by the recent observations of Tat-independent membrane insertion of Tat substrates in vivo and in vitro. Membrane insertion may allow i) a quality control of the folded state by membrane bound proteases like FtsH, ii) the recognition of the membrane spanning signal peptide by Tat system components, and iii) a pulling mechanism of translocation. In some cases of folded Tat substrates, the membrane targeting process may require ATP-dependent N-terminal unfolding-steps.
AB - The twin arginine translocation (Tat) system is a machinery which can translocate folded proteins across energy transducing membranes. Currently it is supposed that Tat substrates bind directly to Tat translocon components before a ΔpH-driven translocation occurs. In this review, an alternative model is presented which proposes that membrane integration could precede Tat-dependent translocation. This idea is mainly supported by the recent observations of Tat-independent membrane insertion of Tat substrates in vivo and in vitro. Membrane insertion may allow i) a quality control of the folded state by membrane bound proteases like FtsH, ii) the recognition of the membrane spanning signal peptide by Tat system components, and iii) a pulling mechanism of translocation. In some cases of folded Tat substrates, the membrane targeting process may require ATP-dependent N-terminal unfolding-steps.
UR - http://www.scopus.com/inward/record.url?scp=0037274388&partnerID=8YFLogxK
U2 - 10.1078/0944-5013-00176
DO - 10.1078/0944-5013-00176
M3 - Review article
C2 - 12608575
AN - SCOPUS:0037274388
VL - 158
SP - 7
EP - 17
JO - Microbiological Research
JF - Microbiological Research
SN - 0944-5013
IS - 1
ER -