The Tat (twin‐arginine translocation) system is a bacterial protein export pathway with the
remarkable ability to transport folded proteins across the cytoplasmic membrane. Preproteins …

We describe the identification of two Escherichia coli genes required for the export of
cofactor‐containing periplasmic proteins, synthesized with signal peptides containing a twin …

The twin-arginine translocation (Tat) protein export system is present in the cytoplasmic
membranes of most bacteria and archaea and has the highly unusual property of transporting …

Background Proteins carrying twin-arginine (Tat) signal peptides are exported into the
periplasmic compartment or extracellular environment independently of the classical Sec-…

Streptomycetes, soil-dwelling mycelial bacteria that form sporulating aerial branches, have
an exceptionally large number of predicted secreted proteins, including many exported via …

Proteins are transported across the bacterial plasma membrane and the chloroplast thylakoid
membrane by means of protein translocases that recognize N-terminal targeting signals in …

In Escherichia coli, transmembrane translocation of proteins can proceed by a number of
routes. A subset of periplasmic proteins are exported via the Tat pathway to which proteins are …

In Escherichia coli a subset of periplasmic proteins is exported through the Tat pathway to
which substrates are directed by an NH 2 -terminal signal peptide containing a consensus …

The Tat system mediates Sec-independent transport of folded precursor proteins across the
bacterial plasma membrane or the chloroplast thylakoid membrane. Tat transport involves …

The Escherichia coli Tat system mediates Sec-independent export of protein precursors
bearing twin arginine signal peptides. Genes known to be involved in this process include tatA, …