Details
| Original language | English |
|---|---|
| Pages (from-to) | 4085-4090 |
| Number of pages | 6 |
| Journal | FEBS Letters |
| Volume | 581 |
| Issue number | 21 |
| Publication status | Published - 21 Aug 2007 |
| Externally published | Yes |
Abstract
Twin-arginine translocation (Tat) systems allow the translocation of folded proteins across biological membranes of most prokaryotes. In proteobacteria, a TatBC complex binds Tat substrates and initiates their translocation after recruitment of the component TatA. TatA and TatB belong to one protein family, but only TatB forms stable complexes with TatC. Here we show that TatB builds up TatA-like modular complexes in the absence of TatC. This TatB ladder ranges from about 100 to over 880 kDa with 105 ± 10 kDa increments. TatC alone can form a 250 kDa complex which could be a scaffold that can recruit TatB to form defined TatBC complexes.
Keywords
- Membrane protein complexes, Protein transport, Translocon assembly, Twin-arginine translocation
ASJC Scopus subject areas
- Biochemistry, Genetics and Molecular Biology(all)
- Biophysics
- Biochemistry, Genetics and Molecular Biology(all)
- Structural Biology
- Biochemistry, Genetics and Molecular Biology(all)
- Biochemistry
- Biochemistry, Genetics and Molecular Biology(all)
- Molecular Biology
- Biochemistry, Genetics and Molecular Biology(all)
- Genetics
- Biochemistry, Genetics and Molecular Biology(all)
- Cell Biology
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In: FEBS Letters, Vol. 581, No. 21, 21.08.2007, p. 4085-4090.
Research output: Contribution to journal › Article › Research › peer review
}
TY - JOUR
T1 - The TatBC complex formation suppresses a modular TatB-multimerization in Escherichia coli
AU - Behrendt, Jana
AU - Lindenstrauß, Ute
AU - Brüser, Thomas
N1 - Funding Information: We are grateful to Jan R. Andreesen for discussions and support. This work was supported by the Graduiertenkolleg 1026 “Conformational transitions in macromolecular interactions” of the Deutsche Forschungsgemeinschaft. Copyright: Copyright 2009 Elsevier B.V., All rights reserved.
PY - 2007/8/21
Y1 - 2007/8/21
N2 - Twin-arginine translocation (Tat) systems allow the translocation of folded proteins across biological membranes of most prokaryotes. In proteobacteria, a TatBC complex binds Tat substrates and initiates their translocation after recruitment of the component TatA. TatA and TatB belong to one protein family, but only TatB forms stable complexes with TatC. Here we show that TatB builds up TatA-like modular complexes in the absence of TatC. This TatB ladder ranges from about 100 to over 880 kDa with 105 ± 10 kDa increments. TatC alone can form a 250 kDa complex which could be a scaffold that can recruit TatB to form defined TatBC complexes.
AB - Twin-arginine translocation (Tat) systems allow the translocation of folded proteins across biological membranes of most prokaryotes. In proteobacteria, a TatBC complex binds Tat substrates and initiates their translocation after recruitment of the component TatA. TatA and TatB belong to one protein family, but only TatB forms stable complexes with TatC. Here we show that TatB builds up TatA-like modular complexes in the absence of TatC. This TatB ladder ranges from about 100 to over 880 kDa with 105 ± 10 kDa increments. TatC alone can form a 250 kDa complex which could be a scaffold that can recruit TatB to form defined TatBC complexes.
KW - Membrane protein complexes
KW - Protein transport
KW - Translocon assembly
KW - Twin-arginine translocation
UR - http://www.scopus.com/inward/record.url?scp=34547699063&partnerID=8YFLogxK
U2 - 10.1016/j.febslet.2007.07.045
DO - 10.1016/j.febslet.2007.07.045
M3 - Article
C2 - 17678896
AN - SCOPUS:34547699063
VL - 581
SP - 4085
EP - 4090
JO - FEBS Letters
JF - FEBS Letters
SN - 0014-5793
IS - 21
ER -