Membrane association of FtsY, the E. coli SRP receptor

• Published in: FEBS letters Vol. 416; no. 3; pp. 225 - 229
• Main Authors: de Leeuw, Erik, Poland, Dennis, Mol, Olaf, Sinning, Irmgard, ten Hagen-Jongman, Corinne M, Oudega, Bauke, Luirink, Joen
• Format: Journal Article
• Language: English
• Published: England Elsevier B.V 27-10-1997
• Subjects: Bacterial Proteins - chemistry; Bacterial Proteins - isolation & purification; Bacterial Proteins - metabolism; Cell Membrane - metabolism; Cloning, Molecular; Cytoplasm - metabolism; endoplasmic reticulum; Escherichia coli; Escherichia coli - genetics; Escherichia coli - metabolism; FtsY; Genetic Complementation Test; GTP; guanosine-5′-phosphate; IPTG; isopropyl-1-thio-β-d-galactopyranoside; Protein targeting; Receptors, Cytoplasmic and Nuclear - chemistry; Receptors, Cytoplasmic and Nuclear - isolation & purification; Receptors, Cytoplasmic and Nuclear - metabolism; Receptors, Peptide - metabolism; Recombinant Proteins - chemistry; Recombinant Proteins - isolation & purification; Recombinant Proteins - metabolism; SDS-PAGE; Signal recognition particle; Signal Recognition Particle - metabolism; sodium dodecyl sulfate-polyacrylamide gel electrophoresis; SRP; SRP receptor; Subcellular Fractions - metabolism; wild-type; SRP; SDS-PAGE; GTP; Signal recognition particle; FtsY; Protein targeting; Escherichia coli; IPTG; ER; WT; SR
• ISSN: 0014-5793; 1873-3468
• DOI: 10.1016/S0014-5793(97)01238-6

FtsY, the
Escherichia coli homologue of the eukaryotic SRP receptor (SRα), is located both in the cytoplasm and in the inner membrane of
E. coli. Similar to SRα, FtsY consists of two major domains: a strongly acidic N-terminal domain (A) and a C-terminal GTP binding domain (NG) of which the crystal structure has recently been determined. The domains were expressed both in vivo and in vitro to examine their subcellular localization. The results suggest that both domains associate with the membrane but that the nature of the association differs.