Cargando…

The TatC component of the twin‐arginine protein translocase functions as an obligate oligomer

The Tat protein export system translocates folded proteins across the bacterial cytoplasmic membrane and the plant thylakoid membrane. The Tat system in E scherichia coli is composed of TatA, TatB and TatC proteins. TatB and TatC form an oligomeric, multivalent receptor complex that binds Tat substr...

Descripción completa

Detalles Bibliográficos
Autores principales:	Cléon, François, Habersetzer, Johann, Alcock, Felicity, Kneuper, Holger, Stansfeld, Phillip J., Basit, Hajra, Wallace, Mark I., Berks, Ben C., Palmer, Tracy
Formato:	Online Artículo Texto
Lenguaje:	English
Publicado:	John Wiley and Sons Inc. 2015
Materias:	Research Articles
Acceso en línea:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5102672/ https://www.ncbi.nlm.nih.gov/pubmed/26112072 http://dx.doi.org/10.1111/mmi.13106

Ejemplares similares

Assembling the Tat protein translocase
por: Alcock, Felicity, et al.
Publicado: (2016)

Characterization of a TatA/TatB binding site on the TatC component of the Escherichia coli twin arginine translocase
por: Severi, Emmanuele, et al.
Publicado: (2023)

Molecular dissection of TatC defines critical regions essential for protein transport and a TatB–TatC contact site
por: Kneuper, Holger, et al.
Publicado: (2012)

TatBC, TatB, and TatC form structurally autonomous units within the twin arginine protein transport system of Escherichia coli
por: Orriss, George L., et al.
Publicado: (2007)

Twin-Arginine Translocation System in Helicobacter pylori: TatC, but Not TatB, Is Essential for Viability
por: Benoit, Stéphane L., et al.
Publicado: (2014)

Transmembrane insertion of twin-arginine signal peptides is driven by TatC and regulated by TatB
por: Fröbel, Julia, et al.
Publicado: (2012)

Diversity and Evolution of Bacterial Twin Arginine Translocase Protein, TatC, Reveals a Protein Secretion System That Is Evolving to Fit Its Environmental Niche
por: Simone, Domenico, et al.
Publicado: (2013)

In vivo experiments do not support the charge zipper model for Tat translocase assembly
por: Alcock, Felicity, et al.
Publicado: (2017)

Substrate-gated docking of pore subunit Tha4 in the TatC cavity initiates Tat translocase assembly
por: Aldridge, Cassie, et al.
Publicado: (2014)

Genetic Evidence for a Tight Cooperation of TatB and TatC during Productive Recognition of Twin-Arginine (Tat) Signal Peptides in Escherichia coli
por: Lausberg, Frank, et al.
Publicado: (2012)

Subunit Organization in the TatA Complex of the Twin Arginine Protein Translocase: A SITE-DIRECTED EPR SPIN LABELING STUDY
por: White, Gaye F., et al.
Publicado: (2010)

Processing by rhomboid protease is required for Providencia stuartii TatA to interact with TatC and to form functional homo-oligomeric complexes
por: Fritsch, Maximilian J, et al.
Publicado: (2012)

New insights into the Tat protein transport cycle from characterizing the assembled Tat translocon
por: Alcock, Felicity, et al.
Publicado: (2022)

Formation of functional Tat translocases from heterologous components
por: Hicks, Matthew G, et al.
Publicado: (2006)

Evolution of mitochondrial TAT translocases illustrates the loss of bacterial protein transport machines in mitochondria
por: Petrů, Markéta, et al.
Publicado: (2018)

Twin-arginine translocase component TatB performs folding quality control via a chaperone-like activity
por: Taw, May N., et al.
Publicado: (2022)

Substrate-triggered position switching of TatA and TatB during Tat transport in Escherichia coli
por: Habersetzer, Johann, et al.
Publicado: (2017)

Signal Peptide Hydrophobicity Modulates Interaction with the Twin-Arginine Translocase
por: Huang, Qi, et al.
Publicado: (2017)

A twin arginine signal peptide and the pH gradient trigger reversible assembly of the thylakoid ΔpH/Tat translocase
por: Mori, Hiroki, et al.
Publicado: (2002)

Analysis of haloarchaeal twin-arginine translocase pathway reveals the diversity of the machineries
por: Ghosh, Deepanjan, et al.
Publicado: (2019)

It takes two to tango: two TatA paralogues and two redox enzyme-specific chaperones are involved in the localization of twin-arginine translocase substrates in Campylobacter jejuni
por: Liu, Yang-Wei, et al.
Publicado: (2014)

Unique Photobleaching Phenomena of the Twin-Arginine Translocase Respiratory Enzyme Chaperone DmsD
por: Rivardo, Fabrizio, et al.
Publicado: (2014)

Unanticipated functional diversity among the TatA-type components of the Tat protein translocase
por: Eimer, Ekaterina, et al.
Publicado: (2018)

Targeting of proteins to the twin‐arginine translocation pathway
por: Palmer, Tracy, et al.
Publicado: (2020)

High Throughput Screen for Escherichia coli Twin Arginine Translocation (Tat) Inhibitors
por: Bageshwar, Umesh K., et al.
Publicado: (2016)

Oligomerization state of the functional bacterial twin-arginine translocation (Tat) receptor complex
por: Sharma, Ankith, et al.
Publicado: (2022)

Envelope Stress Activates Expression of the Twin Arginine Translocation (Tat) System in Salmonella
por: Rogers, Alexandra R., et al.
Publicado: (2022)

A TatABC-Type Tat Translocase Is Required for Unimpaired Aerobic Growth of Corynebacterium glutamicum ATCC13032
por: Oertel, Dan, et al.
Publicado: (2015)

Substrate-Dependent Assembly of the Tat Translocase as Observed in Live Escherichia coli Cells
por: Rose, Patrick, et al.
Publicado: (2013)

Fates of Sec, Tat, and YidC Translocases in Mitochondria and Other Eukaryotic Compartments
por: Petrů, Markéta, et al.
Publicado: (2021)

Probing the quality control mechanism of the Escherichia coli twin-arginine translocase with folding variants of a de novo–designed heme protein
por: Sutherland, George A., et al.
Publicado: (2018)

The Hydrophobic Core of Twin-Arginine Signal Sequences Orchestrates Specific Binding to Tat-Pathway Related Chaperones
por: Shanmugham, Anitha, et al.
Publicado: (2012)

C. elegans TAT-6, a putative aminophospholipid translocase, is expressed in sujc cells in the hermaphrodite gonad.
por: Nilsson, Lars, et al.
Publicado: (2021)

Precursor–Receptor Interactions in the Twin Arginine Protein Transport Pathway Probed with a New Receptor Complex Preparation
por: Wojnowska, Marta, et al.
Publicado: (2018)

Twin-arginine translocation (Tat) mutants in Salmonella enterica serovar Typhimurium have increased susceptibility to cell wall targeting antibiotics
por: M Brauer, Adrienne, et al.
Publicado: (2021)

Prediction of twin-arginine signal peptides
por: Bendtsen, Jannick Dyrløv, et al.
Publicado: (2005)

Molecular Mechanics of RNA Translocases
por: Ding, Steve C., et al.
Publicado: (2012)

Ribosome as a Translocase and Helicase
por: Bao, Chen, et al.
Publicado: (2021)

Secretory production of an FAD cofactor-containing cytosolic enzyme (sorbitol–xylitol oxidase from Streptomyces coelicolor) using the twin-arginine translocation (Tat) pathway of Corynebacterium glutamicum
por: Scheele, Sandra, et al.
Publicado: (2013)

Multipartite control of the DNA translocase, Mfd
por: Smith, Abigail J., et al.
Publicado: (2012)

Cannot write session to /tmp/vufind_sessions/sess_a9kh7jf68884s5uioameb6p8t3