Anionic phospholipids are involved in membrane association of FtsY and stimulate its GTPase activity
AUTOR(ES)
de Leeuw, E.
FONTE
Oxford University Press
RESUMO
FtsY, the Escherichia coli homologue of the eukaryotic signal recognition particle (SRP) receptor α-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.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=305591Documentos Relacionados
- Evidence for coupling of membrane targeting and function of the signal recognition particle (SRP) receptor FtsY
- Neisseria gonorrhoeae PilA Is an FtsY Homolog
- Maize Mutants Lacking Chloroplast FtsY Exhibit Pleiotropic Defects in the Biogenesis of Thylakoid MembranesW⃞
- Association of a cellular myosin II with anionic phospholipids and the neuronal plasma membrane.
- The signal recognition particle receptor of Escherichia coli (FtsY) has a nucleotide exchange factor built into the GTPase domain