Title: Structural organization of the twin-arginine translocation system in Streptomyces lividans
Authors: De Keersmaeker, Sophie ×
Van Mellaert, Lieve
Schaerlaekens, Kristien
Van Dessel, Wesley
Vrancken, Kristof
Lammertyn, Elke
Anné, Jozef
Geukens, Nick #
Issue Date: Jan-2005
Series Title: FEBS Letters vol:579 issue:3 pages:797-802
Abstract: 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.
ISSN: 0014-5793
Publication status: published
KU Leuven publication type: IT
Appears in Collections:Laboratory of Molecular Bacteriology (Rega Institute)
Laboratory for Molecular Cell Biology (-)
Laboratory of Virology and Chemotherapy (Rega Institute)
× corresponding author
# (joint) last author

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