Variable stoichiometry of the TatA component of the twin-arginine protein transport system observed by in vivo single-molecule imaging. - Wikidata - awgldk - TriplyDB

Variable stoichiometry of the TatA component of the twin-arginine protein transport system observed by in vivo single-molecule imaging.

Variable stoichiometry of the TatA component of the twin-arginine protein transport system observed by in vivo single-molecule imaging.

http://www.wikidata.org/entity/Q30483980

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From Animaculum to single molecules: 300 years of the light microscope Inferring diffusion in single live cells at the single-molecule level Substrate-dependent assembly of the Tat translocase as observed in live Escherichia coli cells Supramolecular assemblies underpin turnover of outer membrane proteins in bacteria.Structural model for the protein-translocating element of the twin-arginine transport system Structural Basis for TatA Oligomerization: An NMR Study of Escherichia coli TatA Dimeric Structure Confined Mobility of TonB and FepA in Escherichia coli Membranes.Experimental approaches for addressing fundamental biological questions in living, functioning cells with single molecule precision.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.Assembly dynamics and the roles of FliI ATPase of the bacterial flagellar export apparatus.Visualizing interactions along the Escherichia coli twin-arginine translocation pathway using protein fragment complementation.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 study Mobility of cytoplasmic, membrane, and DNA-binding proteins in Escherichia coli.Multiple precursor proteins bind individual Tat receptor complexes and are collectively transported Signal-dependent turnover of the bacterial flagellar switch protein FliM.Stoichiometry and architecture of active DNA replication machinery in Escherichia coli.Salmonella enterica serovar Enteritidis tatB and tatC mutants are impaired in Caco-2 cell invasion in vitro and show reduced systemic spread in chickens.Characterization of EssB, a protein required for secretion of ESAT-6 like proteins in Staphylococcus aureus Diversity and evolution of bacterial twin arginine translocase protein, TatC, reveals a protein secretion system that is evolving to fit its environmental niche Imaging and quantification of trans-membrane protein diffusion in living bacteria.TatBC-independent TatA/Tat substrate interactions contribute to transport efficiency.Measuring the stoichiometry of functional PspA complexes in living bacterial cells by single molecule photobleaching Stoichiometry for binding and transport by the twin arginine translocation system Diversity and subcellular distribution of archaeal secreted proteins Quantifying Multistate Cytoplasmic Molecular Diffusion in Bacterial Cells via Inverse Transform of Confined Displacement Distribution The 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.Counting protein molecules using quantitative fluorescence microscopy.Single-molecule imaging in live bacteria cells Clustering of C-terminal stromal domains of Tha4 homo-oligomers during translocation by the Tat protein transport system.Twin-arginine translocation system (tat) mutants of Salmonella are attenuated due to envelope defects, not respiratory defects Structural analysis of substrate binding by the TatBC component of the twin-arginine protein transport system.Dynamics of the serine chemoreceptor in the Escherichia coli inner membrane: a high-speed single-molecule tracking study.Substrate-gated docking of pore subunit Tha4 in the TatC cavity initiates Tat translocase assembly.How to quantify protein diffusion in the bacterial membrane.Functioning nanomachines seen in real-time in living bacteria using single-molecule and super-resolution fluorescence imaging.Twin-arginine-dependent translocation of folded proteins.The twin-arginine translocation (Tat) protein export pathway.

P2860

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P2860

Variable stoichiometry of the TatA component of the twin-arginine protein transport system observed by in vivo single-molecule imaging.

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Proceedings of the National Academy of Sciences of the United States of America

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Variable stoichiometry of the ...... vivo single-molecule imaging.

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Grant Buchanan

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Richard M Berry

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Shuyun Chen

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Thierry Granjon

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P2860

Overlapping functions of components of a bacterial Sec-independent protein export pathway

The green fluorescent protein

Localization of the Tat translocon components in Escherichia coli.

Protonation, photobleaching, and photoactivation of yellow fluorescent protein (YFP 10C): a unifying mechanism.

Stoichiometry and turnover in single, functioning membrane protein complexes.

The TatA component of the twin-arginine protein transport system forms channel complexes of variable diameter.

Confined lateral diffusion of membrane receptors as studied by single particle tracking (nanovid microscopy). Effects of calcium-induced differentiation in cultured epithelial cells.

Functional reconstitution of bacterial Tat translocation in vitro

Lateral mobility of proteins in liquid membranes revisited.

Protein translocation across the eukaryotic endoplasmic reticulum and bacterial plasma membranes.

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