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Mircheva, M, Boy, D, Weiche, B, Hucke, F, Graumann, P and Koch, HG (2009) Predominant membrane localization is an essential feature of the bacterial signal recognition particle receptor. BMC Biol. 7:76


The signal recognition particle (SRP) receptor plays a vital role in co-translational protein targeting, because it connects the soluble SRP-ribosome-nascent chain complex (SRP-RNCs) to the membrane bound Sec translocon. The eukaryotic SRP receptor (SR) is a heterodimeric protein complex, consisting of two unrelated GTPases. The SRbeta subunit is an integral membrane protein, which tethers the SRP-interacting SRalpha subunit permanently to the endoplasmic reticulum membrane. The prokaryotic SR lacks the SRbeta subunit and consists of only the SRalpha homologue FtsY. Strikingly, although FtsY requires membrane contact for functionality, cell fractionation studies have localized FtsY predominantly to the cytosolic fraction of Escherichia coli. So far, the exact function of the soluble SR in E. coli is unknown, but it has been suggested that, in contrast to eukaryotes, the prokaryotic SR might bind SRP-RNCs already in the cytosol and only then initiates membrane targeting.


PubMed PMC2780400 Online version:10.1186/1741-7007-7-76


Bacterial Proteins/metabolism; Endoplasmic Reticulum/metabolism; Escherichia coli/physiology; Escherichia coli Proteins/metabolism; Guanosine Triphosphate/metabolism; Intracellular Membranes/metabolism; Microscopy, Fluorescence/methods; Protein Binding; Protein Sorting Signals; Protein Transport; Receptors, Cytoplasmic and Nuclear/metabolism; Receptors, Peptide/metabolism; Ribosomes/metabolism; Signal Recognition Particle/metabolism


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