Details
| Original language | English |
|---|---|
| Pages (from-to) | 135-140 |
| Number of pages | 6 |
| Journal | FEMS Microbiology Letters |
| Volume | 295 |
| Issue number | 1 |
| Publication status | Published - Jun 2009 |
| Externally published | Yes |
Abstract
The twin-arginine translocation (Tat) system serves to translocate folded and often cofactor-containing proteins across biological membranes. The mechanistic limits of the Tat system can be explored by addressing the transport of specifically designed Tat substrates. It thus could be recently shown that unstructured proteins are also accepted by the Tat system, but only if they are polar on their surface. Using the iron-sulfur cofactor-containing model Tat-substrate high potential iron-sulfur protein (HiPIP), we now demonstrate that the bacterial Tat system can translocate small globular proteins even when a long unstructured linker peptide of 110 residues is sandwiched between the signal peptide and the N-terminus of the mature domain. The iron-sulfur cofactor was fully assembled in the transported protein, which demonstrates that HiPIP was folded during translocation. Linker lengths of 148 and 205 residues almost blocked or completely abolished Tat transport, respectively. The tolerance for long unfolded linker peptides challenges our current understanding of the Tat mechanism.
Keywords
- Iron-sulfur cluster, Linker peptide, Protein folding, Protein transport, Twin-arginine translocation
ASJC Scopus subject areas
- Immunology and Microbiology(all)
- Microbiology
- Biochemistry, Genetics and Molecular Biology(all)
- Molecular Biology
- Biochemistry, Genetics and Molecular Biology(all)
- Genetics
Cite this
- Standard
- Harvard
- Apa
- Vancouver
- BibTeX
- RIS
In: FEMS Microbiology Letters, Vol. 295, No. 1, 06.2009, p. 135-140.
Research output: Contribution to journal › Article › Research › peer review
}
TY - JOUR
T1 - Tat transport of linker-containing proteins in Escherichia coli
AU - Lindenstrauß, Ute
AU - Brüser, Thomas
N1 - Copyright: Copyright 2009 Elsevier B.V., All rights reserved.
PY - 2009/6
Y1 - 2009/6
N2 - The twin-arginine translocation (Tat) system serves to translocate folded and often cofactor-containing proteins across biological membranes. The mechanistic limits of the Tat system can be explored by addressing the transport of specifically designed Tat substrates. It thus could be recently shown that unstructured proteins are also accepted by the Tat system, but only if they are polar on their surface. Using the iron-sulfur cofactor-containing model Tat-substrate high potential iron-sulfur protein (HiPIP), we now demonstrate that the bacterial Tat system can translocate small globular proteins even when a long unstructured linker peptide of 110 residues is sandwiched between the signal peptide and the N-terminus of the mature domain. The iron-sulfur cofactor was fully assembled in the transported protein, which demonstrates that HiPIP was folded during translocation. Linker lengths of 148 and 205 residues almost blocked or completely abolished Tat transport, respectively. The tolerance for long unfolded linker peptides challenges our current understanding of the Tat mechanism.
AB - The twin-arginine translocation (Tat) system serves to translocate folded and often cofactor-containing proteins across biological membranes. The mechanistic limits of the Tat system can be explored by addressing the transport of specifically designed Tat substrates. It thus could be recently shown that unstructured proteins are also accepted by the Tat system, but only if they are polar on their surface. Using the iron-sulfur cofactor-containing model Tat-substrate high potential iron-sulfur protein (HiPIP), we now demonstrate that the bacterial Tat system can translocate small globular proteins even when a long unstructured linker peptide of 110 residues is sandwiched between the signal peptide and the N-terminus of the mature domain. The iron-sulfur cofactor was fully assembled in the transported protein, which demonstrates that HiPIP was folded during translocation. Linker lengths of 148 and 205 residues almost blocked or completely abolished Tat transport, respectively. The tolerance for long unfolded linker peptides challenges our current understanding of the Tat mechanism.
KW - Iron-sulfur cluster
KW - Linker peptide
KW - Protein folding
KW - Protein transport
KW - Twin-arginine translocation
UR - http://www.scopus.com/inward/record.url?scp=65449181928&partnerID=8YFLogxK
U2 - 10.1111/j.1574-6968.2009.01600.x
DO - 10.1111/j.1574-6968.2009.01600.x
M3 - Article
C2 - 19473260
AN - SCOPUS:65449181928
VL - 295
SP - 135
EP - 140
JO - FEMS Microbiology Letters
JF - FEMS Microbiology Letters
SN - 0378-1097
IS - 1
ER -