Structural studies of the integral membrane component of the twin-arginine transport system, TatC

Structural studies of the integral membrane component of the twin-arginine transport system, TatC

<p>The twin-arginine protein transport (Tat) system is one of two general protein transport systems in the cytoplasmic membranes of bacteria, and is conserved in the thylakoid membranes of plants. The Tat system transports fully folded proteins of varying sizes across the membrane. This feat i...

Bibliografski detalji
Glavni autor:	Rollauer, SE
Daljnji autori:	Lea, S
Format:	Disertacija
Jezik:	English
Izdano:	2013
Teme:	Biochemistry

Slični predmeti

Structure of the TatC core of the twin-arginine protein transport system.
od: Rollauer, SE, i dr.
Izdano: (2012)

Structure of the TatC core of the twin-arginine protein transport system
od: Rollauer, SE, i dr.
Izdano: (2012)

TatBC, TatB, and TatC form structurally autonomous units within the twin arginine protein transport system of Escherichia coli.
od: Orriss, G, i dr.
Izdano: (2007)

Investigation of Escherichia coli Tat (twin arginine translocase) transport in vitro
od: Yong, S
Izdano: (2011)

Genetic evidence for a TatC dimer at the core of the Escherichia coli twin arginine (Tat) protein translocase.
od: Maldonado, B, i dr.
Izdano: (2011)

Molecular dissection of TatC defines critical regions essential for protein transport and a TatB-TatC contact site
od: Kneuper, H, i dr.
Izdano: (2012)

Genetic evidence for a tight cooperation of TatB and TatC during productive recognition of twin-arginine (Tat) signal peptides in Escherichia coli.
od: Frank Lausberg, i dr.
Izdano: (2012-01-01)

Twin-Arginine Translocation System in <named-content content-type="genus-species">Helicobacter pylori</named-content>: TatC, but Not TatB, Is Essential for Viability
od: Stéphane L. Benoit, i dr.
Izdano: (2014-02-01)

Diversity and evolution of bacterial twin arginine translocase protein, TatC, reveals a protein secretion system that is evolving to fit its environmental niche.
od: Domenico Simone, i dr.
Izdano: (2013-01-01)

Structural analysis of substrate binding by the TatBC component of the twin-arginine protein transport system.
od: Tarry, M, i dr.
Izdano: (2009)

Characterisation of the membrane-extrinsic domain of the TatB component of the twin arginine protein translocase.
od: Maldonado, B, i dr.
Izdano: (2011)

Processing by rhomboid protease is required for Providencia stuartii TatA to interact with TatC and to form functional homo-oligomeric complexes
od: Fritsch, M, i dr.
Izdano: (2012)

Live cell imaging shows reversible assembly of the TatA component of the twin-arginine protein transport system.
od: Alcock, F, i dr.
Izdano: (2013)

Variable stoichiometry of the TatA component of the twin-arginine protein transport system observed by in vivo single-molecule imaging.
od: Leake, M, i dr.
Izdano: (2008)

The twin-arginine translocation (Tat) protein export pathway
od: Palmer, T, i dr.
Izdano: (2012)

Single-molecule fluorescence microscopy of the twin-arginine translocation (Tat) system
od: Leake, M, i dr.
Izdano: (2007)

Structure and function of bacterial proteins secreted by the type three secretion and twin arginine translocation pathways
od: Lillington, J, i dr.
Izdano: (2011)

Structural studies of integral membrane GPCR accessory proteins
od: Sladek, B
Izdano: (2013)

Envelope Stress Activates Expression of the Twin Arginine Translocation (Tat) System in Salmonella
od: Alexandra R. Rogers, i dr.
Izdano: (2022-10-01)

Cysteine-scanning mutagenesis and disulfide mapping studies of the conserved domain of the twin-arginine translocase TatB component.
od: Lee, P, i dr.
Izdano: (2006)

Memprotmd: adding the grease to membrane protein structures
od: Stansfeld, P, i dr.
Izdano: (2012)

Oligomerization state of the functional bacterial twin-arginine translocation (Tat) receptor complex
od: Ankith Sharma, i dr.
Izdano: (2022-09-01)

High Throughput Screen for Escherichia coli Twin Arginine Translocation (Tat) Inhibitors.
od: Umesh K Bageshwar, i dr.
Izdano: (2016-01-01)

Twin-arginine translocase component TatB performs folding quality control via a chaperone-like activity
od: May N. Taw, i dr.
Izdano: (2022-09-01)

Biophysical studies of membrane protein structure and function
od: Dijkman, P, i dr.
Izdano: (2014)

Tat-fimbriae (“tafi”): An unusual type of haloarchaeal surface structure depending on the twin-arginine translocation pathway
od: Anna V. Galeva, i dr.
Izdano: (2025-02-01)

Structural studies of a membrane embedded chloride channel from E.Coli, a prokaryotic homologue of ClC channels
od: Bowler, M, i dr.
Izdano: (2001)

Membrane structure/
od: Michell R. H.
Izdano: (1981)

Analysis of Tat targeting function and twin-arginine signal peptide activity in Escherichia coli.
od: Palmer, T, i dr.
Izdano: (2010)

Protocol for an in vitro assay to study HIV-1 Tat methylation
od: Daniela Boehm, i dr.
Izdano: (2023-12-01)

Arginine methylation of the p30 C/EBPα oncoprotein regulates progenitor proliferation and myeloid differentiation
od: Linh T. Nguyen, i dr.
Izdano: (2024-11-01)

Modelling the influence of ligand binding towards the structure and dynamics of protein arginine deiminase IV
od: Ibrahim, Zalikha
Izdano: (2017)

Structural and functional studies with native mass spectrometry — insights into membranes and glycoproteins
od: Chen, S
Izdano: (2022)

Structural and biochemical characterisation of human integral membrane proteins regarded as potential therapeutic targets
od: da Costa Cabral Gomes Páscoa, T
Izdano: (2022)

High resolution structural studies of membrane proteins using solid state NMR
od: Aslimovska, L
Izdano: (2008)

Structural studies of the shortest extended synaptotagmin with only two C2 domains from Trypanosoma brucei
od: Emma Stepinac, i dr.
Izdano: (2021-05-01)

Structure and association of ATP-binding cassette transporter nucleotide-binding domains
od: Kerr, I
Izdano: (2002)

Multiscale simulations of lipid interactions with integral membrane proteins: aquaporins
od: Stansfeld, P, i dr.
Izdano: (2011)

A signal sequence suppressor mutant that stabilizes an assembled state of the twin arginine translocase
od: Huang, Q, i dr.
Izdano: (2017)

Comprehensive identification of arginine methylation in primary T cells reveals regulatory roles in cell signalling
od: Geoghegan, V, i dr.
Izdano: (2015)