期刊
FEBS LETTERS
卷 581, 期 21, 页码 4091-4097出版社
WILEY
DOI: 10.1016/j.febslet.2007.07.044
关键词
twin arginine; Tat; protein transport; blue native-PAGE; membrane proteins
资金
- Biotechnology and Biological Sciences Research Council [BB/D011140/1, BB/D000386/1, BB/D011140/2, BB/C516144/1] Funding Source: researchfish
- Medical Research Council [G117/519] Funding Source: researchfish
- BBSRC [BB/C516144/1, BB/D011140/1, BB/D011140/2] Funding Source: UKRI
- MRC [G117/519] Funding Source: UKRI
- Biotechnology and Biological Sciences Research Council [BB/D011140/1, BB/D000386/1, P16795, BB/D011140/2, BB/C516144/1] Funding Source: Medline
- Medical Research Council [G117/519] Funding Source: Medline
- Wellcome Trust Funding Source: Medline
The Tat (twin arginine translocation) system transports folded proteins across bacterial and thylakoid membranes. The integral membrane proteins TatA, TatB, and TatC are the essential components of the Tat pathway in Escherichia coli. We demonstrate that formation of a stable complex between TatB and TatC does not require TatA or other Tat components. We show that the TatB and TatC proteins are each able to a form stable, defined, homomultimeric complexes. These we suggest correspond to structural subcomplexes within the parental TatBC complex. We infer that TatC forms a core to the TatBC complex on to which TatB assembles. (c) 2007 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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