PMID:10675322
| Citation |
de Leeuw, E, te Kaat, K, Moser, C, Menestrina, G, Demel, R, de Kruijff, B, Oudega, B, Luirink, J and Sinning, I (2000) Anionic phospholipids are involved in membrane association of FtsY and stimulate its GTPase activity. EMBO J. 19:531-41 |
|---|---|
| Abstract |
FtsY, the Escherichia coli homologue of the eukaryotic signal recognition particle (SRP) receptor alpha-subunit, is located in both the cytoplasm and inner membrane. It has been proposed that FtsY has a direct targeting function, but the mechanism of its association with the membrane is unclear. FtsY is composed of two hydrophilic domains: a highly charged N-terminal domain (the A-domain) and a C-terminal GTP-binding domain (the NG-domain). FtsY does not contain any hydrophobic sequence that might explain its affinity for the inner membrane, and a membrane-anchoring protein has not been detected. In this study, we provide evidence that FtsY interacts directly with E.coli phospholipids, with a preference for anionic phospholipids. The interaction involves at least two lipid-binding sites, one of which is present in the NG-domain. Lipid association induced a conformational change in FtsY and greatly enhanced its GTPase activity. We propose that lipid binding of FtsY is important for the regulation of SRP-mediated protein targeting. |
| Links |
PubMed PMC305591 Online version:10.1093/emboj/19.4.531 |
| Keywords |
Anions; Bacterial Proteins/chemistry; Bacterial Proteins/metabolism; Binding Sites; Cell Membrane/metabolism; Escherichia coli/metabolism; GTP Phosphohydrolases/chemistry; GTP Phosphohydrolases/metabolism; Guanosine Diphosphate/pharmacology; Guanosine Triphosphate/pharmacology; Liposomes; Phospholipids/chemistry; Phospholipids/metabolism; Protein Binding; Protein Conformation; Protein Structure, Tertiary; Receptors, Cytoplasmic and Nuclear/chemistry; Receptors, Cytoplasmic and Nuclear/metabolism; Signal Recognition Particle/chemistry; Signal Recognition Particle/metabolism; Static Electricity |
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