The PrlA and PrlG phenotypes are caused by a loosened association among the translocase SecYEG subunits. - Wikidata - awgldk - TriplyDB

The PrlA and PrlG phenotypes are caused by a loosened association among the translocase SecYEG subunits.

The PrlA and PrlG phenotypes are caused by a loosened association among the translocase SecYEG subunits.

http://www.wikidata.org/entity/Q33891061

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SecA, a remarkable nanomachine The conformation of a signal peptide bound by Escherichia coli preprotein translocase SecA SecA alone can promote protein translocation and ion channel activity: SecYEG increases efficiency and signal peptide specificity Posttranslational protein translocation across the membrane of the endoplasmic reticulum.Escherichia coli translocase: the unravelling of a molecular machine.Dynamics of SecY translocons with translocation-defective mutations The SecYEG preprotein translocation channel is a conformationally dynamic and dimeric structure Evaluating the oligomeric state of SecYEG in preprotein translocase.A novel class of secA alleles that exert a signal-sequence-dependent effect on protein export in Escherichia coli.Escherichia coli SecG is required for residual export mediated by mutant signal sequences and for SecY-SecE complex stability Probing the SecYEG translocation pore size with preproteins conjugated with sizable rigid spherical molecules.Stability and function of the Sec61 translocation complex depends on the Sss1p tail-anchor sequence A prl mutation in SecY suppresses secretion and virulence defects of Listeria monocytogenes secA2 mutants Different modes of SecY-SecA interactions revealed by site-directed in vivo photo-cross-linking.Translocation channel gating kinetics balances protein translocation efficiency with signal sequence recognition fidelity Position-dependent effects of polylysine on Sec protein transport A little help from my friends: quality control of presecretory proteins in bacteria Emerging themes in SecA2-mediated protein export.Dissecting structures and functions of SecA-only protein-conducting channels: ATPase, pore structure, ion channel activity, protein translocation, and interaction with SecYEG/SecDF•YajC.Structural Similarities and Differences between Two Functionally Distinct SecA Proteins, Mycobacterium tuberculosis SecA1 and SecA2.Interactions that drive Sec-dependent bacterial protein transport.Breaking on through to the other side: protein export through the bacterial Sec system.Investigating the SecY plug movement at the SecYEG translocation channel.Preprotein translocation by a hybrid translocase composed of Escherichia coli and Bacillus subtilis subunits.Projection structure and oligomeric properties of a bacterial core protein translocase.Dissociation of the dimeric SecA ATPase during protein translocation across the bacterial membrane.A SecE mutation that modulates SecY-SecE translocase assembly, identified as a specific suppressor of SecY defects Biochemical characterization of a mutationally altered protein translocase: proton motive force stimulation of the initiation phase of translocation.Binding, activation and dissociation of the dimeric SecA ATPase at the dimeric SecYEG translocase.Unlocking the Bacterial SecY Translocon.Conformational dynamics of the plug domain of the SecYEG protein-conducting channel.Immobilization of the plug domain inside the SecY channel allows unrestricted protein translocation.YidC and SecYEG form a heterotetrameric protein translocation channel.Mapping the sites of interaction between SecY and SecE by cysteine scanning mutagenesis.The core of the bacterial translocase harbors a tilted transmembrane segment 3 of SecE.Superactive SecY variants that fulfill the essential translocation function with a reduced cellular quantity.Defective translocation of a signal sequence mutant in a prlA4 suppressor strain of Escherichia coli.The Sec System: Protein Export in Escherichia coli.SecYEG proteoliposomes catalyze the Deltaphi-dependent membrane insertion of FtsQ.Both transmembrane domains of SecG contribute to signal sequence recognition by the Escherichia coli protein export machinery.

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P2860

The PrlA and PrlG phenotypes are caused by a loosened association among the translocase SecYEG subunits.

http://www.wikidata.org/entity/Q33891061

description

1999 nî lūn-bûn

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1999 թուականի Յունիսին հրատարակուած գիտական յօդուած

@hyw

1999 թվականի հունիսին հրատարակված գիտական հոդված

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1999年の論文

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1999年論文

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1999年論文

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1999年論文

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1999年論文

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1999年論文

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1999年论文

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The PrlA and PrlG phenotypes a ...... e translocase SecYEG subunits.

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The PrlA and PrlG phenotypes a ...... e translocase SecYEG subunits.

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The PrlA and PrlG phenotypes a ...... e translocase SecYEG subunits.

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The PrlA and PrlG phenotypes a ...... e translocase SecYEG subunits.

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The PrlA and PrlG phenotypes a ...... e translocase SecYEG subunits.

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The EMBO Journal

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The PrlA and PrlG phenotypes a ...... e translocase SecYEG subunits.

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P2093

F Duong

http://www.w3.org/2001/XMLSchema#string

W Wickner

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P2860

Evolutionary conservation of components of the protein translocation complex

Tom7 modulates the dynamics of the mitochondrial outer membrane translocase and plays a pathway-related role in protein import

The sec and prl genes of Escherichia coli

The Sec system.

SecA protein, a peripheral protein of the Escherichia coli plasma membrane, is essential for the functional binding and translocation of proOmpA.

Purified secB protein of Escherichia coli retards folding and promotes membrane translocation of the maltose-binding protein in vitro.

secG and temperature modulate expression of azide-resistant and signal sequence suppressor phenotypes of Escherichia coli secA mutants.

Distinct catalytic roles of the SecYE, SecG and SecDFyajC subunits of preprotein translocase holoenzyme.

The SecDFyajC domain of preprotein translocase controls preprotein movement by regulating SecA membrane cycling.

PrlA4 prevents the rejection of signal sequence defective preproteins by stabilizing the SecA-SecY interaction during the initiation of translocation.

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3263-3270

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scholarly article

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10.1093/EMBOJ/18.12.3263

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12

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18

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1999-06-01T00:00:00Z

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12928733

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10369667

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1171407

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