TY - JOUR T1 - Structural organization of the twin-arginine translocation system in Streptomyces lividans. JF - FEBS Lett Y1 - 2005 A1 - De Keersmaeker, Sophie A1 - Van Mellaert, Lieve A1 - Schaerlaekens, Kristien A1 - Wesley Van Dessel A1 - Vrancken, Kristof A1 - Lammertyn, Elke A1 - Anné, Jozef A1 - Geukens, Nick KW - Arginine KW - Base Sequence KW - Blotting, Western KW - Cytoplasm KW - DNA Primers KW - Electrophoresis, Polyacrylamide Gel KW - Membrane Transport Proteins KW - Protein Conformation KW - Streptomyces lividans AB -

The twin-arginine translocation (Tat) system exports folded proteins across bacterial cytoplasmic membranes. Recently, genes encoding TatA, TatB and TatC homologues were identified in Streptomyces lividans and the functionality of the Tat pathway was demonstrated. Here, we have examined the localization and structural organization of the Tat components in S. lividans. Interestingly, besides being membrane-associated proteins, S. lividans TatA and TatB were also detected in the cytoplasm. TatC could only be detected in isolated membrane fractions. Whereas all TatC was found to be stably inserted in the membrane, part of membrane-associated TatA and TatB could be extracted following high salt, sodium carbonate or urea treatment suggesting a more loose association with the membrane. Finally, we have analyzed Tat complexes that could be purified from an S. lividans TatABC overproducing strain. From the cytoplasmic membrane, two types of high molecular mass Tat complexes could be isolated having a similar composition as those isolated from Escherichia coli. In the cytoplasm, TatA and TatB were detected as monomer or as homo-oligomeric complexes.

VL - 579 CP - 3 U1 - https://www.ncbi.nlm.nih.gov/pubmed/15670849?dopt=Abstract M3 - 10.1016/j.febslet.2004.12.059 ER -