Oligomers of Tha4 organize at the thylakoid Tat translocase during protein transport.
about
Targeting of lumenal proteins across the thylakoid membraneSubstrate-dependent assembly of the Tat translocase as observed in live Escherichia coli cellsStructure of the TatC core of the twin-arginine protein transport systemStructural model for the protein-translocating element of the twin-arginine transport systemStructural Basis for TatA Oligomerization: An NMR Study of Escherichia coli TatA Dimeric StructureVariable stoichiometry of the TatA component of the twin-arginine protein transport system observed by in vivo single-molecule imaging.Dynamic localization of Tat protein transport machinery components in Streptomyces coelicolor.Live cell imaging shows reversible assembly of the TatA component of the twin-arginine protein transport system.Formation of functional Tat translocases from heterologous componentsTranslocation of a phycoerythrin alpha subunit across five biological membranes.Pleiotropic effects of the twin-arginine translocation system on biofilm formation, colonization, and virulence in Vibrio cholerae.TatA complexes exhibit a marked change in organisation in response to expression of the TatBC complex.Subunit organization in the TatA complex of the twin arginine protein translocase: a site-directed EPR spin labeling studyMultiple precursor proteins bind individual Tat receptor complexes and are collectively transportedTatBC-independent TatA/Tat substrate interactions contribute to transport efficiency.Evidence for a dynamic and transient pathway through the TAT protein transport machineryThe chloroplast twin arginine transport (Tat) component, Tha4, undergoes conformational changes leading to Tat protein transport.Intra-plastid protein trafficking: how plant cells adapted prokaryotic mechanisms to the eukaryotic condition.Mechanisms of protein import into thylakoids of chloroplasts.Plastid protein import and sorting: different paths to the same compartments.Escherichia coli tatC mutations that suppress defective twin-arginine transporter signal peptides.Clustering of C-terminal stromal domains of Tha4 homo-oligomers during translocation by the Tat protein transport system.Structural analysis of substrate binding by the TatBC component of the twin-arginine protein transport system.Protein transport in organelles: Protein transport into and across the thylakoid membrane.Interconvertibility of lipid- and translocon-bound forms of the bacterial Tat precursor pre-SufI.A signal sequence suppressor mutant that stabilizes an assembled state of the twin arginine translocase.Substrate-gated docking of pore subunit Tha4 in the TatC cavity initiates Tat translocase assembly.Twin-arginine-dependent translocation of folded proteins.The twin-arginine translocation (Tat) protein export pathway.Functional Tat transport of unstructured, small, hydrophilic proteins.Mechanistic Aspects of Folded Protein Transport by the Twin Arginine Translocase (Tat).Twin-Arginine Protein Translocation.Functional analysis of the twin-arginine translocation pathway in Corynebacterium glutamicum ATCC 13869.Assembling the Tat protein translocase.The canonical twin-arginine translocase components are not required for secretion of folded green fluorescent protein from the ancestral strain of Bacillus subtilis.Salt sensitivity of minimal twin arginine translocases.Early contacts between substrate proteins and TatA translocase component in twin-arginine translocation.Co-factor insertion and disulfide bond requirements for twin-arginine translocase-dependent export of the Bacillus subtilis Rieske protein QcrA.The TatC component of the twin-arginine protein translocase functions as an obligate oligomer.Initial assembly steps of a translocase for folded proteins.
P2860
Q27002662-AFC3CE69-CAF4-4739-9064-B149ED8ED789Q27311011-0A0EAB59-ECE2-4B8C-A266-51A9AB8DB4EEQ27675340-B4856A1C-7459-4C5B-A026-E998C276E870Q27676737-331107C9-B6E0-430C-A630-93866613814DQ27684932-3D33D504-3034-4372-927F-00CA86A909A6Q30483980-9E93B90A-6F55-4500-B41F-B74254D69949Q30527854-9C8F1C13-31A4-4FE9-A757-7E7D53913A61Q30546248-BD1A4BC0-4BD7-4C85-8371-D4E31C458426Q33251032-65B8CE8C-7738-449B-A9B2-08059CF9D452Q33294324-C2917304-2099-465A-B223-6DFBE5FED511Q33456259-FD48156D-3C59-47CF-A97E-DA70178A73D8Q33577532-4C3253F2-3701-4074-AA2D-C543D04DDAD8Q33593832-120F2136-F3B4-446B-A2D9-113B60C1378AQ33878456-6C580690-7671-4FA1-82E5-D8815C1F0DD7Q35577950-2C6A5794-366B-43A6-95B7-DA81951D2A09Q35880616-2E068751-8CC7-4026-BA6A-DE0CCB79044FQ36298510-A6288DA0-E11A-4EBA-B6FC-028BB2070BACQ36346841-B660CE67-39E8-4999-8114-EDEE3E02B300Q36909231-644B8895-C117-4231-A287-5A2C5C15EC77Q37066814-4787985D-F4BE-44AE-8C2A-035DC700D463Q37141701-9779721B-990F-4DB6-A8C3-3D903C52998FQ37146697-3D2FD81D-CD00-4B00-A33A-428AA11C42FCQ37281583-8D28E57B-0076-4C91-8F7B-48C21538B4C4Q37383485-2911F738-EB42-4DB1-ADE1-25B2B2CD4666Q37404850-DB13395C-C031-48D8-82CD-738D6EA1B3D0Q37696002-F27267B3-D23C-4ABD-AEA8-BA51BA3E8E12Q37703474-B293431D-B7DB-4E78-B596-0B71B833B9A5Q37993035-9E2A52D4-F3D2-4879-931C-89EBC63C08BAQ38017546-AE85B87A-CB9B-490F-8C12-684F9872FC17Q38298400-7F8DFE59-E968-414D-8212-4BD19D6A7890Q38480343-A933884A-C374-47DB-8A43-6B678FDB0376Q38819418-06D2D40D-47C5-4A6A-A2A6-E78D8EE77BFEQ39108709-E39A9E1F-E2C1-4B4C-AAAD-93EEEA2C3528Q39134196-F7BB5F0B-2FC5-4E2F-8160-EE89DB27D277Q39541017-C4394B3A-753D-4938-8EC2-2475323CC76EQ39935919-F26E4EE6-F7A0-4AD7-AD6B-8F0F15894CE3Q39936045-01FB4BEE-3A13-4F25-9F89-2C554C116F86Q39999263-C7921D95-E6D5-473C-9384-4F8E33114239Q40796436-1B700989-F15C-4C14-8636-5FD57AC51855Q40842405-C9B7EF42-F557-4F7B-8F14-EDF3B8A67EB4
P2860
Oligomers of Tha4 organize at the thylakoid Tat translocase during protein transport.
description
2005 nî lūn-bûn
@nan
2005年の論文
@ja
2005年学术文章
@wuu
2005年学术文章
@zh
2005年学术文章
@zh-cn
2005年学术文章
@zh-hans
2005年学术文章
@zh-my
2005年学术文章
@zh-sg
2005年學術文章
@yue
2005年學術文章
@zh-hant
name
Oligomers of Tha4 organize at the thylakoid Tat translocase during protein transport.
@en
Oligomers of Tha4 organize at the thylakoid Tat translocase during protein transport.
@nl
type
label
Oligomers of Tha4 organize at the thylakoid Tat translocase during protein transport.
@en
Oligomers of Tha4 organize at the thylakoid Tat translocase during protein transport.
@nl
prefLabel
Oligomers of Tha4 organize at the thylakoid Tat translocase during protein transport.
@en
Oligomers of Tha4 organize at the thylakoid Tat translocase during protein transport.
@nl
P2860
P356
P1476
Oligomers of Tha4 organize at the thylakoid Tat translocase during protein transport
@en
P2093
Hiroki Mori
Kenneth Cline
P2860
P304
P356
10.1074/JBC.M512453200
P407
P577
2005-12-30T00:00:00Z