The core Escherichia coli signal recognition particle receptor contains only the N and G domains of FtsY.
Previous studies have proposed that the N-terminal A domain (approximately 200 amino acid residues) of the Escherichia coli signal recognition particle (SRP) receptor, FtsY, is required for membrane targeting. In contrast to this suggestion, we show that A domain-truncated versions of FtsY, harboring only domains N and G, are functional. Therefore, we propose that N and G domains constitute the core SRP receptor.
Eitan
Asa
A
Department of Biological Chemistry, Weizmann Institute of Science, Rehovot 76100, Israel.
Bibi
Eitan
E
D001426:Bacterial Proteins / Q000032:analysis / Q000235:genetics / Q000378:metabolism*; D015153:Blotting, Western; D002462:Cell Membrane / Q000378:metabolism; D004926:Escherichia coli / Q000378:metabolism*; D029968:Escherichia coli Proteins / Q000032:analysis / Q000235:genetics / Q000378:metabolism*; D005816:Genetic Complementation Test; D017434:Protein Structure, Tertiary; D018160:Receptors, Cytoplasmic and Nuclear / Q000032:analysis / Q000235:genetics / Q000378:metabolism*; D018271:Signal Recognition Particle / Q000378:metabolism
D001426:Bacterial Proteins; D029968:Escherichia coli Proteins; C087406:FtsY protein, Bacteria; D018160:Receptors, Cytoplasmic and Nuclear; D018271:Signal Recognition Particle