Fluorescence resonance energy transfer analysis of protein translocase. SecYE from Thermus thermophilus HB8 forms a constitutive oligomer in membranes.
about
Two translocating hydrophilic segments of a nascent chain span the ER membrane during multispanning protein topogenesisX-ray structure of a protein-conducting channelConformational transition of Sec machinery inferred from bacterial SecYE structuresPurification, crystallization and preliminary X-ray diffraction of SecDF, a translocon-associated membrane protein, from Thermus thermophilus.Molecular dynamics studies of the archaeal translocon.Different modes of SecY-SecA interactions revealed by site-directed in vivo photo-cross-linking.The ribosome and YidC. New insights into the biogenesis of Escherichia coli inner membrane proteins.A single copy of SecYEG is sufficient for preprotein translocation.Cotranslational membrane protein biogenesis at the endoplasmic reticulum.Nanodiscs unravel the interaction between the SecYEG channel and its cytosolic partner SecA.Bacterial protein translocation requires only one copy of the SecY complex in vivo.Sec-dependent protein translocation across biological membranes: evolutionary conservation of an essential protein transport pathway (review).Oligomeric states of the SecA and SecYEG core components of the bacterial Sec transloconStoichiometry of SecYEG in the active translocase of Escherichia coli varies with precursor species.Membrane chaperone SecDF plays a role in the secretion of Listeria monocytogenes major virulence factors.Bacterial Sec protein transport is rate-limited by precursor length: a single turnover study.Crystallization and preliminary X-ray diffraction of the first periplasmic domain of SecDF, a translocon-associated membrane protein, from Thermus thermophilusSize, motion, and function of the SecY translocon revealed by molecular dynamics simulations with virtual probes.Investigating the SecY plug movement at the SecYEG translocation channel.Binding, activation and dissociation of the dimeric SecA ATPase at the dimeric SecYEG translocase.SecY-SecA fusion protein retains the ability to mediate protein transport.Visualization of distinct entities of the SecYEG translocon during translocation and integration of bacterial proteinsEnvironmental transition of signal-anchor sequences during membrane insertion via the endoplasmic reticulum translocon.The way is the goal: how SecA transports proteins across the cytoplasmic membrane in bacteria.The TatA component of the twin-arginine translocation system locally weakens the cytoplasmic membrane of Escherichia coli upon protein substrate binding.
P2860
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P2860
Fluorescence resonance energy transfer analysis of protein translocase. SecYE from Thermus thermophilus HB8 forms a constitutive oligomer in membranes.
description
2003 nî lūn-bûn
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name
Fluorescence resonance energy ...... itutive oligomer in membranes.
@en
Fluorescence resonance energy ...... itutive oligomer in membranes.
@nl
type
label
Fluorescence resonance energy ...... itutive oligomer in membranes.
@en
Fluorescence resonance energy ...... itutive oligomer in membranes.
@nl
prefLabel
Fluorescence resonance energy ...... itutive oligomer in membranes.
@en
Fluorescence resonance energy ...... itutive oligomer in membranes.
@nl
P2093
P2860
P356
P1476
Fluorescence resonance energy ...... titutive oligomer in membranes
@en
P2093
Arthur E Johnson
Koreaki Ito
Ryoji Masui
Seiki Kuramitsu
Tomoya Tsukazaki
Yoshiaki Kimura
Yoshinori Akiyama
P2860
P304
14257-14264
P356
10.1074/JBC.M300230200
P407
P577
2003-01-17T00:00:00Z