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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.

Original publication

DOI

10.1016/j.febslet.2007.07.044

Type

Journal article

Journal

FEBS Lett

Publication Date

21/08/2007

Volume

581

Pages

4091 - 4097

Keywords

Escherichia coli, Escherichia coli Proteins, Membrane Transport Proteins, Multiprotein Complexes, Protein Binding, Protein Transport