Signal sequence-independent SRP-SR complex formation at the membrane suggests an alternative targeting pathway within the SRP cycle.
about
Structural basis of signal sequence surveillance and selection by the SRP–FtsY complexYlxM is a newly identified accessory protein that influences the function of signal recognition particle pathway components in Streptococcus mutansStructure of the quaternary complex between SRP, SR, and translocon bound to the translating ribosome.Regulation of cargo recognition, commitment, and unloading drives cotranslational protein targetingDynamic interaction of the sec translocon with the chaperone PpiDSignal recognition particle and SecA cooperate during export of secretory proteins with highly hydrophobic signal sequences.Ribosome-SRP-FtsY cotranslational targeting complex in the closed statePromiscuous targeting of polytopic membrane proteins to SecYEG or YidC by the Escherichia coli signal recognition particle.SecYEG activates GTPases to drive the completion of cotranslational protein targeting.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.The C-terminal regions of YidC from Rhodopirellula baltica and Oceanicaulis alexandrii bind to ribosomes and partially substitute for SRP receptor function in Escherichia coli.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.YidC and SecYEG form a heterotetrameric protein translocation channel.The interaction network of the YidC insertase with the SecYEG translocon, SRP and the SRP receptor FtsY.The signal recognition particle contacts uL23 and scans substrate translation inside the ribosomal tunnel.Dynamic switch of the signal recognition particle from scanning to targeting.
P2860
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P2860
Signal sequence-independent SRP-SR complex formation at the membrane suggests an alternative targeting pathway within the SRP cycle.
description
2011 nî lūn-bûn
@nan
2011年の論文
@ja
2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
2011年论文
@zh
2011年论文
@zh-cn
name
Signal sequence-independent SR ...... pathway within the SRP cycle.
@en
Signal sequence-independent SR ...... pathway within the SRP cycle.
@nl
type
label
Signal sequence-independent SR ...... pathway within the SRP cycle.
@en
Signal sequence-independent SR ...... pathway within the SRP cycle.
@nl
prefLabel
Signal sequence-independent SR ...... pathway within the SRP cycle.
@en
Signal sequence-independent SR ...... pathway within the SRP cycle.
@nl
P2093
P2860
P356
P1476
Signal sequence-independent SR ...... pathway within the SRP cycle.
@en
P2093
David Braig
Eli O van der Sluis
Hans-Georg Koch
Ilie Sachelaru
Lukas Sturm
Miryana Mircheva
Roland Beckmann
P2860
P304
P356
10.1091/MBC.E11-02-0152
P577
2011-05-05T00:00:00Z