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Membrane interactions and self‐association of the TatA and TatB components of the twin‐arginine translocation pathway
Author(s) -
De Leeuw Erik,
Porcelli Ida,
Sargent Frank,
Palmer Tracy,
Berks Ben C.
Publication year - 2001
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(01)02904-0
Subject(s) - twin arginine translocation pathway , tatb , arginine , transmembrane protein , membrane , chemistry , biophysics , membrane protein , biochemistry , chromosomal translocation , cytoplasm , helix (gastropod) , transport protein , membrane transport protein , biology , amino acid , gene , ecology , detonation , receptor , organic chemistry , snail , explosive material
The Escherichia coli Tat system mediates Sec‐independent export of protein precursors bearing twin‐arginine signal peptides. The essential Tat pathway components TatA, TatB and TatC are shown to be integral membrane proteins. Upon removal of the predicted N‐terminal transmembrane helix TatA becomes a water‐soluble protein. In contrast the homologous TatB protein retains weak peripheral interactions with the cytoplasmic membrane when the analogous helix is deleted. Chemical crosslinking studies indicate that TatA forms at least homotrimers, and TatB minimally homodimers, in the native membrane environment. The presence of such homo‐oligomeric interactions is supported by size exclusion chromatography.