A mutant hunt for defects in membrane protein assembly yields mutations affecting the bacterial signal recognition particle and Sec machinery
about
Structural basis of signal sequence surveillance and selection by the SRP–FtsY complexSecretion of LamB-LacZ by the signal recognition particle pathway of Escherichia coliEffect of sequences of the active-site dipeptides of DsbA and DsbC on in vivo folding of multidisulfide proteins in Escherichia coli.Genetic analysis of the twin arginine translocator secretion pathway in bacteria.Membrane protein biogenesis in Ffh- or FtsY-depleted Escherichia coli.Inhibition of bacterial disulfide bond formation by the anticoagulant warfarin.Sec-dependent membrane protein insertion: sequential interaction of nascent FtsQ with SecY and YidC.The Haloferax volcanii FtsY homolog is critical for haloarchaeal growth but does not require the A domain.Target-directed proteolysis at the ribosome.New prospects in studying the bacterial signal recognition particle pathway.Biogenesis of inner membrane proteins in Escherichia coli.Genetic screen yields mutations in genes encoding all known components of the Escherichia coli signal recognition particle pathway.Critical regions of secM that control its translation and secretion and promote secretion-specific secA regulation.Functional analysis of the signal recognition particle in Escherichia coli by characterization of a temperature-sensitive ffh mutant.The targeting pathway of Escherichia coli presecretory and integral membrane proteins is specified by the hydrophobicity of the targeting signalSignal recognition particle and SecA cooperate during export of secretory proteins with highly hydrophobic signal sequences.Compounds targeting disulfide bond forming enzyme DsbB of Gram-negative bacteria.Translation elongation regulates substrate selection by the signal recognition particle.Complex behavior in solution of homodimeric SecA.A channel connecting the mother cell and forespore during bacterial endospore formation.Characterization of conserved bases in 4.5S RNA of Escherichia coli by construction of new F' factorsSpecificity of SecYEG for PhoA precursors and SecA homologs on SecA protein-conducting channels.Roles of a conserved arginine residue of DsbB in linking protein disulfide-bond-formation pathway to the respiratory chain of Escherichia coli.Genetic suppressors and recovery of repressed biochemical memory.Methionine sulfoxide reductases protect Ffh from oxidative damages in Escherichia coli.Biogenesis of MalF and the MalFGK(2) maltose transport complex in Escherichia coli requires YidC.Binding Protein-Dependent Uptake of Maltose into Cells via an ATP-Binding Cassette Transporter.Identification of ZipA, a signal recognition particle-dependent protein from Neisseria gonorrhoeae.The DsbA signal sequence directs efficient, cotranslational export of passenger proteins to the Escherichia coli periplasm via the signal recognition particle pathway.SRP-dependent co-translational targeting and SecA-dependent translocation analyzed as individual steps in the export of a bacterial protein.Yersinia enterocolitica type III secretion of YopR requires a structure in its mRNAEscherichia coli SRP, its protein subunit Ffh, and the Ffh M domain are able to selectively limit membrane protein expression when overexpressed.The variable subdomain of Escherichia coli SecA functions to regulate SecA ATPase activity and ADP release.Use of thioredoxin as a reporter to identify a subset of Escherichia coli signal sequences that promote signal recognition particle-dependent translocation.Export of the pseudopilin XcpT of the Pseudomonas aeruginosa type II secretion system via the signal recognition particle-Sec pathway.Signal recognition particle-dependent inner membrane targeting of the PulG Pseudopilin component of a type II secretion system.Contribution of the FtsQ transmembrane segment to localization to the cell division site.Escherichia coli SecA helicase activity is not required in vivo for efficient protein translocation or autogenous regulation.Two-stage binding of SecA to the bacterial translocon regulates ribosome-translocon interaction.Copper stress causes an in vivo requirement for the Escherichia coli disulfide isomerase DsbC.
P2860
Q27677237-40819DBB-BA60-48CD-8136-93E026C85636Q28775689-B641570D-D6FD-44C6-84EE-851EA7E36D85Q30981412-26590624-1A67-481A-9027-DDB46AE2D3AEQ31059440-E4445D66-A831-4A58-84F0-DBE1BE819C33Q33531769-29168EDE-C6E8-4783-B5E8-936255CF6263Q33591624-BC2947C9-E32E-4A20-AD0A-D9F26680CAFCQ33757388-CA059B95-0952-4D53-B271-2C902ED054D6Q33855609-C6E2C208-F477-4D5D-AA38-54CE2E0D7FEDQ33934301-A76CA8B2-70F2-4458-84FE-A2769BC8EB69Q34109335-154184DB-E907-40EA-B61C-B5250D97668DQ34222736-47F7BE4E-A95A-472F-BF3B-126C9CF68548Q34304210-3296BEB1-DB37-497D-96CF-CE39BC793625Q34309801-8051DAFF-EE2C-472F-B377-8F0B0E502AE7Q34310953-03FC1625-C8FF-4D25-8C44-7C18F288CD38Q34741147-4475091A-00AD-4510-897F-17ABE9C7704BQ35143704-CE1D185C-D21A-4A36-A156-D69BED5F5913Q35196256-310FD288-F2B0-4A5D-8D1F-116969C9D158Q35801999-032B9039-B745-4AA6-8CFA-5158EFEA40BAQ36639172-93D8F0A0-D982-4756-86A4-63B136F53E27Q36937179-494A0659-3FBA-481F-A7B6-4759778C8740Q36974562-BA472268-ADA2-4A64-AC29-04FB05A1CE11Q37087214-52A995A0-3847-4D0E-8D78-FFD5E06528B5Q37264681-70304098-E09C-4EA8-AD3D-86C249702A89Q37364322-1BC415A8-5015-423A-9006-5A17F7458615Q37616996-017CA3CF-DF11-4A0D-A994-0BB1A598C844Q38291259-C6B957B4-D29C-4312-8224-C45B987DFDA2Q38601256-F61E43EB-0778-4AB8-BDC6-C76630D13DD5Q39739652-BB3E24DB-C30A-4CB7-A13D-07B8E5D543BFQ39887818-FBBBA26E-D297-4762-818C-E35A0AA21D8CQ40388434-C8FB5ACF-73C6-4320-B398-A3934C77C849Q41441370-A0B2219B-2BF1-423E-BF96-049A038E23D3Q42085172-B99D4F36-9B9C-4E3F-A13D-C880D1B15B5AQ42152267-AFD12646-45B4-4F72-ADAA-DC60234739CDQ42723141-B2077F27-33A3-42F2-81AE-226EBE2612EAQ42845566-87FA7F73-798A-4364-B951-D0EDBEFE7DDEQ42845651-CB7C2A15-8D7C-4658-8AFF-F1FBD1901238Q42909832-9DD478EA-93C0-402B-83A0-7C1E9A80C49EQ43690465-47F1C57C-7157-434C-8986-57E9E50E395AQ44542398-AEB3E247-778B-4D91-8940-4C74B13E7BEDQ46640858-F434F55A-94DD-4F3A-86AA-F7CF9331979D
P2860
A mutant hunt for defects in membrane protein assembly yields mutations affecting the bacterial signal recognition particle and Sec machinery
description
2000 nî lūn-bûn
@nan
2000年の論文
@ja
2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
@zh-tw
2000年论文
@wuu
2000年论文
@zh
2000年论文
@zh-cn
name
A mutant hunt for defects in m ...... ion particle and Sec machinery
@ast
A mutant hunt for defects in m ...... ion particle and Sec machinery
@en
type
label
A mutant hunt for defects in m ...... ion particle and Sec machinery
@ast
A mutant hunt for defects in m ...... ion particle and Sec machinery
@en
prefLabel
A mutant hunt for defects in m ...... ion particle and Sec machinery
@ast
A mutant hunt for defects in m ...... ion particle and Sec machinery
@en
P2093
P2860
P356
P1476
A mutant hunt for defects in m ...... ion particle and Sec machinery
@en
P2093
P2860
P304
P356
10.1073/PNAS.090087297
P407
P577
2000-04-01T00:00:00Z