Subunit interactions in the twin-arginine translocase complex of Escherichia coli
UNSPECIFIED. (2000) Subunit interactions in the twin-arginine translocase complex of Escherichia coli. FEBS LETTERS, 472 (1). pp. 88-92. ISSN 0014-5793Full text not available from this repository.
A subset of Escherichia coli proteins, in particular cofactor-binding proteins with so-called twin-arginine signal peptides, is transported to the periplasm via the twin-arginine translocation (Tat) pathway. The tatA and tatB genes encode important components of the export system and we have analysed whether the proteins encoded by these genes physically interact, Using co-immunoprecipitation experiments, we show that TatA and TatB do indeed associate with each other. Gel filtration chromatograph demonstrates that both proteins are present in a large complex with an apparent molecular mass of approximately 600 kDa, indicating the presence of other components and/or several TatA and TatB subunits, Finally, we show that TatA is stable in the absence of TatB and may participate in a separate complex lacking TatB in wild-type cells, (C) 2000 Federation of European Biochemical Societies.
|Item Type:||Journal Article|
|Subjects:||Q Science > QD Chemistry
Q Science > QH Natural history > QH301 Biology
|Journal or Publication Title:||FEBS LETTERS|
|Publisher:||ELSEVIER SCIENCE BV|
|Date:||21 April 2000|
|Number of Pages:||5|
|Page Range:||pp. 88-92|
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