Membrane binding of the bacterial signal recognition particle receptor involves two distinct binding sites
about
Structures of the signal recognition particle receptor from the archaeon Pyrococcus furiosus: implications for the targeting step at the membraneAn interaction between the SRP receptor and the translocon is critical during cotranslational protein translocation.Predominant membrane localization is an essential feature of the bacterial signal recognition particle receptor.Dynamic interaction of the sec translocon with the chaperone PpiDBiophysical studies of the membrane-embedded and cytoplasmic forms of the glucose-specific Enzyme II of the E. coli phosphotransferase system (PTS).Lipid activation of the signal recognition particle receptor provides spatial coordination of protein targeting.Molecular mechanism of co-translational protein targeting by the signal recognition particleProtein targeting by the signal recognition particle.Ribosome-SRP-FtsY cotranslational targeting complex in the closed stateConformational changes in the GTPase modules of the signal reception particle and its receptor drive initiation of protein translocationDynamics of co-translational protein targeting.Mammalian SRP receptor switches the Sec61 translocase from Sec62 to SRP-dependent translocationSecYEG activates GTPases to drive the completion of cotranslational protein targeting.Mechanisms of YidC-mediated insertion and assembly of multimeric membrane protein complexes.SRP RNA controls a conformational switch regulating the SRP-SRP receptor interaction.Signal recognition particle: an essential protein-targeting machine.Co-translational protein targeting to the bacterial membrane.The Sec translocon mediated protein transport in prokaryotes and eukaryotes.Signal recognition particle (SRP) and SRP receptor: a new paradigm for multistate regulatory GTPases.Electrostatics and Intrinsic Disorder Drive Translocon Binding of the SRP Receptor FtsY.Ribosome binding induces repositioning of the signal recognition particle receptor on the translocon.Two-step membrane binding by the bacterial SRP receptor enable efficient and accurate Co-translational protein targeting.Visualization of distinct entities of the SecYEG translocon during translocation and integration of bacterial proteinsDepletion of the signal recognition particle receptor inactivates ribosomes in Escherichia coli.YidC occupies the lateral gate of the SecYEG translocon and is sequentially displaced by a nascent membrane protein.Signal sequence-independent SRP-SR complex formation at the membrane suggests an alternative targeting pathway within the SRP cycle.The membrane-binding motif of the chloroplast signal recognition particle receptor (cpFtsY) regulates GTPase activity.Conformation of the signal recognition particle in ribosomal targeting complexes.In vitro reconstitution of co-translational D1 insertion reveals a role of the cpSec-Alb3 translocase and Vipp1 in photosystem II biogenesis.The bacterial SRP receptor, FtsY, is activated on binding to the translocon.Membrane targeting of ribosomes and their release require distinct and separable functions of FtsY.Escherichia coli signal recognition particle receptor FtsY contains an essential and autonomous membrane-binding amphipathic helix.The Bacterial SRP Receptor, SecA and the Ribosome Use Overlapping Binding Sites on the SecY Translocon
P2860
Q27438158-1B27EEA0-D1EE-4EC9-8763-1CDFE3B6BE72Q27932958-AE7ABAB9-2B57-4342-B419-4B1199E9A242Q30491773-9AA5BCDE-0881-4DA8-BFD4-DEF65A6E342CQ33985391-D0A4EF8F-258F-4716-AF0C-BD2393E7AF1CQ34025993-9F1EC4CC-2953-4E81-B854-BA5B4CCC0858Q34083157-B3F5172A-9364-494D-8660-057999A99E31Q34797147-6684FF1E-4124-480F-9B8A-5B280DD81212Q34989260-23C66706-D9FC-4901-A737-764627848D0CQ35279475-885C14A4-0371-42B1-92AB-DEFC80B27EB1Q36118866-3285E211-6857-4468-B35B-3FBF16AD063FQ36385101-248CD2CC-8235-46FC-898A-5F3D84098F95Q36392449-319DF635-8394-4DFA-9853-FC9309735228Q36618916-BBBA3D85-E5BD-4A2B-97A4-E388219E92DCQ37227948-E6A9B4D8-673B-498A-BE4F-42EC85BC1587Q37399396-9D6EC56B-DC28-49D3-B9AD-4FDD5EDD52DBQ38081948-3DAF85AF-654A-4B2B-8D87-4466DF103897Q38186912-29CFB5EC-4718-43F0-A17B-2184776D83E7Q38206834-BFB3BDF9-DBF6-4FBA-918C-A03C3D340439Q40978065-B96A2728-1FAF-4A26-83BD-63B48A3A134EQ41664177-E9E20D5D-8F06-442B-A658-E0F55991898DQ41867811-8DFA4571-721E-4A93-9DE1-9E4363FD7AEAQ41886358-643B5295-56E1-4D95-88B6-A597FC6E0356Q41960890-D789A641-C5BA-4FA3-B933-45A148087578Q41965856-98270CEB-F73B-4F5D-8261-048AAE16A26AQ42144026-6411CE5B-7367-48E6-BC8A-F1A6AB431C5FQ42277688-FBDA4BA5-CF11-4932-9EE8-C87EAFA83989Q43123368-D2397A3B-25A0-4D60-B83F-5A2BB3C5EDF5Q43214650-8E24B1D5-8EE4-436F-AEA4-782E6BDABE37Q50216151-466756DF-E13B-4D92-91C3-B2E29465EB82Q51674537-4779A91E-CD69-493B-BB87-C9979DD3FF21Q54435409-CDC36699-30D0-4EDE-90F7-5876A92FFA96Q54435413-9C2F847C-6553-471A-8775-B83DE8ACB8F8Q57830682-A62FF286-E6C2-4546-8DCF-8DF43925581D
P2860
Membrane binding of the bacterial signal recognition particle receptor involves two distinct binding sites
description
2006 nî lūn-bûn
@nan
2006年の論文
@ja
2006年論文
@yue
2006年論文
@zh-hant
2006年論文
@zh-hk
2006年論文
@zh-mo
2006年論文
@zh-tw
2006年论文
@wuu
2006年论文
@zh
2006年论文
@zh-cn
name
Membrane binding of the bacter ...... ves two distinct binding sites
@ast
Membrane binding of the bacter ...... ves two distinct binding sites
@en
type
label
Membrane binding of the bacter ...... ves two distinct binding sites
@ast
Membrane binding of the bacter ...... ves two distinct binding sites
@en
prefLabel
Membrane binding of the bacter ...... ves two distinct binding sites
@ast
Membrane binding of the bacter ...... ves two distinct binding sites
@en
P2093
P2860
P356
P1476
Membrane binding of the bacter ...... ves two distinct binding sites
@en
P2093
Emile Schiltz
Hans-Georg Koch
Sandra Angelini
P2860
P304
P356
10.1083/JCB.200606093
P407
P577
2006-08-21T00:00:00Z