The role of complex formation between the Escherichia coli hydrogenase accessory factors HypB and SlyD.
about
Evaluation of two homologous proline-rich proteins of Coccidioides posadasii as candidate vaccines against coccidioidomycosisRapA, the SWI/SNF subunit of Escherichia coli RNA polymerase, promotes the release of nascent RNA from transcription complexes.A subset of the diverse COG0523 family of putative metal chaperones is linked to zinc homeostasis in all kingdoms of life.Rhizobium leguminosarum hupE encodes a nickel transporter required for hydrogenase activity.Synthesis of the 2Fe subcluster of the [FeFe]-hydrogenase H cluster on the HydF scaffold.Optimized E. coli expression strain LOBSTR eliminates common contaminants from His-tag purificationMaturation of Rhizobium leguminosarum hydrogenase in the presence of oxygen requires the interaction of the chaperone HypC and the scaffolding protein HupKAn intact urease assembly pathway is required to compete with NikR for nickel ions in Helicobacter pylori.Common themes and unique proteins for the uptake and trafficking of nickel, a metal essential for the virulence of Helicobacter pyloriSpecific metal recognition in nickel trafficking.Metal transfer within the Escherichia coli HypB-HypA complex of hydrogenase accessory proteins.High-affinity metal binding by the Escherichia coli [NiFe]-hydrogenase accessory protein HypB is selectively modulated by SlyD.Metallochaperones and metalloregulation in bacteria.Protein interactions and localization of the Escherichia coli accessory protein HypA during nickel insertion to [NiFe] hydrogenase.Escherichia coli SlyD, more than a Ni(II) reservoir.Metal selectivity of the Escherichia coli nickel metallochaperone, SlyD.UreE-UreG complex facilitates nickel transfer and preactivates GTPase of UreG in Helicobacter pylori.Multifaceted SlyD from Helicobacter pylori: implication in [NiFe] hydrogenase maturation.The peptidyl-prolyl isomerase activity of SlyD is not required for maturation of Escherichia coli hydrogenase.In vivo interactome of Helicobacter pylori urease revealed by tandem affinity purification.Interaction of SlyD with HypB of Helicobacter pylori facilitates nickel trafficking.Relationship between the GTPase, metal-binding, and dimerization activities of E. coli HypB.Nickel translocation between metallochaperones HypA and UreE in Helicobacter pylori.The Escherichia coli metal-binding chaperone SlyD interacts with the large subunit of [NiFe]-hydrogenase 3.His-rich sequences – is plagiarism from nature a good idea?
P2860
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P2860
The role of complex formation between the Escherichia coli hydrogenase accessory factors HypB and SlyD.
description
2007 nî lūn-bûn
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2007年の論文
@ja
2007年学术文章
@wuu
2007年学术文章
@zh
2007年学术文章
@zh-cn
2007年学术文章
@zh-hans
2007年学术文章
@zh-my
2007年学术文章
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2007年學術文章
@yue
2007年學術文章
@zh-hant
name
The role of complex formation ...... cessory factors HypB and SlyD.
@en
The role of complex formation ...... cessory factors HypB and SlyD.
@nl
type
label
The role of complex formation ...... cessory factors HypB and SlyD.
@en
The role of complex formation ...... cessory factors HypB and SlyD.
@nl
prefLabel
The role of complex formation ...... cessory factors HypB and SlyD.
@en
The role of complex formation ...... cessory factors HypB and SlyD.
@nl
P2860
P356
P1476
The role of complex formation ...... cessory factors HypB and SlyD.
@en
P2093
Jie Wei Zhang
Michael R Leach
P2860
P304
16177-16186
P356
10.1074/JBC.M610834200
P407
P577
2007-04-10T00:00:00Z