DnaK plays a pivotal role in Tat targeting of CueO and functions beside SlyD as a general Tat signal binding chaperone.
about
A microbial sensor for discovering structural probes of protein misfolding and aggregationStructural diversity in twin-arginine signal peptide-binding proteinsThe global responses of Mycobacterium tuberculosis to physiological levels of copperIdentification of functional Tat signal sequences in Mycobacterium tuberculosis proteinsCtpV: a putative copper exporter required for full virulence of Mycobacterium tuberculosisA stromal pool of TatA promotes Tat-dependent protein transport across the thylakoid membrane.Strategies for successful recombinant expression of disulfide bond-dependent proteins in Escherichia coli.Visualizing interactions along the Escherichia coli twin-arginine translocation pathway using protein fragment complementation.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.The hydrophobic core of twin-arginine signal sequences orchestrates specific binding to Tat-pathway related chaperones.Detrimental effect of the 6 His C-terminal tag on YedY enzymatic activity and influence of the TAT signal sequence on YedY synthesis.Use of folding modulators to improve heterologous protein production in Escherichia coli.Interconvertibility of lipid- and translocon-bound forms of the bacterial Tat precursor pre-SufI.The twin-arginine translocation system: contributions to the pathobiology of Campylobacter jejuni.Twin-arginine-dependent translocation of folded proteins.Protein interactions and localization of the Escherichia coli accessory protein HypA during nickel insertion to [NiFe] hydrogenase.Signal Peptide Hydrophobicity Modulates Interaction with the Twin-Arginine Translocase.A bacterial two-hybrid system based on the twin-arginine transporter pathway of E. coliApplication of an E. coli signal sequence as a versatile inclusion body tagThe Tat system for membrane translocation of folded proteins recruits the membrane-stabilizing Psp machinery in Escherichia coli.The Tat Substrate CueO Is Transported in an Incomplete Folding StateMultifaceted SlyD from Helicobacter pylori: implication in [NiFe] hydrogenase maturation.DmsD, a Tat system specific chaperone, interacts with other general chaperones and proteins involved in the molybdenum cofactor biosynthesis.Biochemical characterization of two Azotobacter vinelandii FKBPs and analysis of their interaction with the small subunit of carbamoyl phosphate synthetase.Role of vesicle-inducing protein in plastids 1 in cpTat transport at the thylakoid.In vivo interactome of Helicobacter pylori urease revealed by tandem affinity purification.The Escherichia coli metal-binding chaperone SlyD interacts with the large subunit of [NiFe]-hydrogenase 3.
P2860
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P2860
DnaK plays a pivotal role in Tat targeting of CueO and functions beside SlyD as a general Tat signal binding chaperone.
description
2007 nî lūn-bûn
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name
DnaK plays a pivotal role in T ...... Tat signal binding chaperone.
@en
DnaK plays a pivotal role in T ...... Tat signal binding chaperone.
@nl
type
label
DnaK plays a pivotal role in T ...... Tat signal binding chaperone.
@en
DnaK plays a pivotal role in T ...... Tat signal binding chaperone.
@nl
prefLabel
DnaK plays a pivotal role in T ...... Tat signal binding chaperone.
@en
DnaK plays a pivotal role in T ...... Tat signal binding chaperone.
@nl
P2093
P2860
P356
P1476
DnaK plays a pivotal role in T ...... Tat signal binding chaperone.
@en
P2093
Angelika Schierhorn
Thomas Brüser
Wenke Graubner
P2860
P304
P356
10.1074/JBC.M608235200
P407
P577
2007-01-10T00:00:00Z