Trends in Biochemical Sciences
News & CommentPutative integral membrane SRP receptors
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Cited by (32)
Co-Translational Membrane Targeting and Holo-Translocon Docking of Ribosomes Translating the SRP Receptor
2022, Journal of Molecular BiologyCitation Excerpt :Intriguingly, although both proteins (NG + 1 and NG) are able to target the membrane in vivo,24,31 only NG + 1 interacts with membrane vesicles in vitro,25 suggesting that co-translational targeting of NG is a prerequisite for its membrane docking. This is also supported by several observations in the bacterial32–34 and mammalian35 systems, which raised the possibility that FtsY and its eukaryotic homolog target the membrane co-translationally. This, along with additional considerations,36 have led to the hypothesis that FtsY may constitutively target ribosomes to the membrane during its own translation.
Is there a twist in the Escherichia coli signal recognition particle pathway?
2012, Trends in Biochemical SciencesEarly targeting events during membrane protein biogenesis in Escherichia coli
2011, Biochimica et Biophysica Acta - BiomembranesCitation Excerpt :This question depends on whether or not FtsY needs to be targeted to membranes co-translationally for efficient biological activity. In any case, this and other studies disfavor the possibility that soluble FtsY plays a critical role in the targeting pathway [35,111,112]. Are hydrophobic nascent polypeptides necessary for targeting SRP–RNCs to membrane bound FtsY in vivo and in vitro?
Genetic evidence for functional interaction of the Escherichia coli signal recognition particle receptor with acidic lipids in vivo
2010, Journal of Biological ChemistryCitation Excerpt :Targeting of ribosomes to the cytoplasmic membrane in Escherichia coli requires the signal recognition particle (SRP)3 receptor, FtsY (3). Many reports have suggested that FtsY functions as a membrane-bound receptor (4, 5), despite the fact that it has no known membrane anchor partner homologous to the mammalian β-subunit of the SRP receptor (SR-β). In agreement with this, previous studies showed that FtsY interacts with membrane-bound ribosomes (6) and the translocon (7) and that its membrane localization is required for its function (4, 5, 8).
Two Cooperating Helices Constitute the Lipid-binding Domain of the Bacterial SRP Receptor
2009, Journal of Molecular BiologyA Cleavable N-Terminal Membrane Anchor is Involved in Membrane Binding of the Escherichia coli SRP Receptor
2008, Journal of Molecular Biology