SecYEG Assembles Into A Tetramer To Form The Active Protein Translocation Channel

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SecA, a remarkable nanomachine - CyberLeninka

by I Kusters 2011 Cited by 85 (2000) SecYEG assembles into a tetramer to form the active protein translocation channel. EMBO J 19(5):852 861. 20. Scheuring J, Braun N, 

Biogenesis of inner membrane proteins in Escherichia coli

19 Dec 2011 structure, it has been proposed that a single SecYEG heterotrimer forms the active translocation channel. A recent biophysical study.

Break on through to the other side the Sec translocon

Biol. 285, 1789 1800. 13 Manting, E.H. et al. (2000) SecYEG assembles into a tetramer to form the active protein translocation channel. EMBO J. 19, 852 861.

Protein targeting, translocation and insertion in - DiVA Portal

by L Baars 2007 Cited by 2 translocation through the channel by hydrolysis of ATP (4) (adapted from [61]). trimeric and tetrameric assemblies of the SecYEG-complex have been.

SecYEG assembles into a tetramer to form the active protein

by EH Manting 2000 Cited by 246 of the nucleotide-modulated structural changes of the soluble SecA molecule demonstrate that it exists in a. Translocase mediates preprotein translocation 

Directed evolution designed to optimize the in vivo protein

by S Quan 2010 Chapter two is modified from my previous publication ―The CXXC motif is more than a redox rheostat‖1 on the work of complementing DsbA with active site- 

Bacterial secretome: the assembly manual and operating

by A Economou 2002 Cited by 73 Driessen, A. J., 2000, SecYEG assembles into a tetramer to form the active protein translocation channel. EMBO Journal, 19, 852 ±.

Integrating Protein Homeostasis Strategies in Prokaryotes

by A Mogk 2011 Cited by 78 cause perturbation in protein homeostasis and lead to protein misfolding. Bacteria have folded form that is activated for assembly into the ribosome.

A Novel Class of secA Alleles That Exert a Signal - Genetics

by K Khatib 2002 Cited by 12 High-level expression of PAI2::AP chimeric proteins from the arabinose SecYEG is either monomeric teins are maintained in a translocation-competent con-.

Protein secretion and outer membrane assembly in

by X Gatsos 2008 Cited by 99 folding and assembly of b-barrel proteins in bacterial outer membranes. These recent studies build on classic studies of protein secretion in bacteria, 

Caractérisation moléculaire du système de sécrétion de type II

by W Xiaohui 2012 the stepwise translocation of preprotein across the SecYEG channel in the bacterial IM into a tetramer to form the active protein translocation channel.

Membrane proteins

by CN Chin 2002 Cited by 22 protein translocation. Cell 87, 721 732. 15 Manting, E.H. et al. (2000) SecYEG assembles into a tetramer to form the active protein translocation channel.

The Conformational Gymnastics of the Escherichia Coli SecA

by JL Maki 2009 mimics the translocation-active form of SecA. (TM) segment of the protein leaves the SecYEG channel and associates with YidC. The.

Recombinant protein secretion in Escherichia coli - The

by FJM Mergulhao 2005 Cited by 569 Manting EH, van Der Does C, Remigy H, Engel A, Driessen AJ. SecYEG assembles into a tetramer to form the active protein translocation channel.

Glycolipozyme MPIase is essential for topology - PNAS

by M Moser 2013 Cited by 30 a translocation ATPase, play central roles in preprotein trans- SecYEG forms oligomers, such as a dimer and a tetramer (9 12). In some 

60Mb - Warwick WRAP - University of Warwick

1.1 Protein transport in bacteria The two complexes only come together to form an active translocon upon substrate binding and in presence of PMF.

Early Steps in Cotranslational Translocation of Proteins across

by A Neuhof 2000 translocated across the ER membrane through a hydrophilic channel formed by the mammals and S. cerevisiae and the purified SecYEG complex all assemble 

Pilus chaperones represent a novel type of protein folding

by M Vetsch 2004 assembles into a long rigid helical rod and the subunits FimF, FimG, and FimH, forming a tetramer to form the active protein translocation channel.

X-ray structure of a protein-conducting channel - Molecular

by B van den Berg Cited by 1396 Manting, E. H., van Der Does, C., Remigy, H., Engel, A. & Driessen, A. J. SecYEG assembles into a tetramer to form the active protein translocation channel.9 pages

University of Groningen SecYEG assembles into a tetramer to

SecYEG assembles into a tetramer to form the active protein translocation channel. Manting, E.H; van der Does, C.; Remiy, H.; Engel, A.; Driessen, A.J.M.;  11 pages

Deciphering the Role of YidC in Bacterial Membrane Protein

by M Chen 2002 transporters, channels, and ATPases, they must be targeted to their correct SecYEG assembles into a tetramer to form the active protein translocation.

β-Barrel Membrane Protein Assembly by the Bam Complex

by CL Hagan 2011 Cited by 311 membrane proteins in the cell in order to efficiently transport them tetramer to form the active protein translocation channel.

Protein Traffic in Gramnegative bacteria how exported and

by RE Dalbey 2012 Cited by 100 Gram-negative bacteria assemble many proteins into the inner and outer mem- translocation through the SecYEG channel (Fig. 2).

Twin-arginine-dependent translocation of folded proteins

by J Fröbel 2012 Cited by 88 Twin-arginine translocation (Tat) denotes a protein transport pathway in bacteria, archaea and type proteins form homo- and hetero-oligomeric complexes.

Dynamic Structure of the Translocon SecYEG in Membrane

by RRS Gari 2013 Cited by 36 These SecYEG proteoliposomes were active in translocation (2000) SecYEG assembles into a tetramer to form the active protein trans-.

The role of lipids in membrane insertion and translocation of

SecYEG forms the actual translocation channel through the membrane and SecYEG assembles into a tetramer to form the active protein trans- location 

The protein-conducting channel SecYEG - CiteSeerX

by AKJ Veenendaal 2004 Cited by 172 multimeric protein complex that assembles into oligomeric forms. Active transport of molecules, such as proteins, into or across the 

The TatC component of the twinarginine protein translocase

by F Cléon 2015 Cited by 28 SecY forms the protein transport channel (Van den SecYEG complexes in detergent solution, or following reconstitution into liposomes 

INVESTIGATING COTRANSLATIONAL - OAKTrust

by CG JONGSMA 2008 Most membrane proteins in eukaryotic cells are co-translationally SecYEG assembles into a tetramer to form the active protein translocation channel.

structural and functional characterization of mulitdrug

by L Yu 2013 The active sites or translocation pathway of the protein is located at the inter-subunit surface. The potassium channel KcsA is such an 

Structural Investigations of the Protein Export System at the

In contrast, co-assembly of SecA and SecYEG into liposomes increased the plug has an ability to leave the channel during protein transport and return 

Assembly of the translocase motor onto the preprotein

by S Karamanou 2008 Cited by 30 Driessen, A.J. (2000) SecYEG assembles into a tetramer to form the active protein translocation channel. EMBO J. 19: 852 861.

Download - Kent Academic Repository - University of Kent

by AS Jones 2017 Cited by 1 The Twin Arginine Translocase (Tat) is one of two protein translocation mechanisms in assembles into a tetramer to form the active protein translocation 

In vitro studies on the SecA involvement in the assembly of an

by R Antonoaea Translocation of secretory proteins across the SecYEG translocon the dimeric forms of SecYEG are assembled into tetrameric structures upon the.

Development of methods for study of membrane proteins in

surfactants have detrimental effects on protein form and function. SecYEG: The bacterial translocon, responsible for translocation and insertion of 

Disulfide bridge formation between SecY and a translocating

by KS Cannon 2005 Cited by 193 Whether this channel forms at the interface of multiple SecYEG assembles into a tetramer to form the active protein transloca-.

Transfer of the Ribosome-Nascent Chain Complex to the

by Y Jiang 2007 forms the protein-conducting channel in both pathways. Sec61p complex assembles an oligomer to mediate protein translocation, actually.

Membrane Protein Insertion in Bacteria from a Structural

by M Paetzel 2005 Cited by 1 40. Manting EH, van Der Does C, Remigy H et al. SecYEG assembles into a tetramer to form the active protein translocation channel.

Dissertation - Heidelberg University

by O Schlenker 2006 Cited by 1 chain is inserted into the protein conducting channel (PCC, translocon). SecYEG assembles into a tetramer to form the active protein translocation.

Three-dimensional structure of SecYEG - Page d'accueil de l

by C Breyton Cited by 344 report the structure of the Escherichia coli SecYEG assembly at an in-plane resolution of 8A˚ tetramer to form the active protein translocation channel.

Architecture of the SecYEG-DF-YajC-YidC Holotranslocon

by M Botte 2013 Both pathways converge at the protein-conducting channel SecYEG. involving targeting, translocation, folding and assembly of complexes.

Download book PDF

Soluble proteins convert into aggregates under denaturing conditions Assembly Modulation of Channel-forming Peptides. 87. S. Futaki. 7.1. Introduction.

Nucleotide Binding Induces Changes in the Oligomeric State

by Z Bu 2003 Cited by 76 In Escherichia coli, SecA is a large, multifunctional protein that is a vital tetramer to form the active protein translocation channel.

Uniqueness of the mechanism of protein import into the

by S Léon 1763 Cited by 131 proteins were unfolded during translocation and assembled on the matrix side. the apparent movement of active catalase (a tetramer) from the.

Architecture of the Ribosome Channel Complex Derived from

by JF Menetret 2005 Cited by 163 SecYEG assembles into a tetramer to form the active protein translocation channel. EMBO J. 19, 852 861. 6. Ménétret, J. F., Neuhof, A., Morgan, D. G., 

Construction of an efficient secretion system for recombinant

by KC Leite Cited by 2 1.2.2 The protein-conducting channel: SecYEG Driessen,A.J.M. (2000) SecYEG assembles into a tetramer to form the active protein translocation channel.

This electronic thesis or dissertation has been downloaded

associates with a ubiquitous channel SecYEG where it drives the post- SecYEG assembles into a tetramer to form the active protein translocation channel.

Alphaproteobacteria - ScienceOpen

by X Gatsos 2008 Cited by 99 folding and assembly of b-barrel proteins in bacterial outer membranes. These recent studies build on classic studies of protein secretion in bacteria, 

Functional Cooperativity among the Subunits of the

by A Horner 2016 monomer possesses a channel that facilitates the transport of water across the membrane, and yet the protein assembles into a tetramer.

Structural Studies of Eukaryotic Ribosome Biogenesis and the

10 Jul 2020 chain complex, require folding of proteins in one compartment before translocation across a membrane to allow the protein to be active in