The replication initiation protein of the broad-host-range plasmid RK2 is activated by the ClpX chaperone.
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Replisome Assembly at Bacterial Chromosomes and Iteron PlasmidsMitochondrial ClpX Activates a Key Enzyme for Heme Biosynthesis and Erythropoiesis.Effects of protein stability and structure on substrate processing by the ClpXP unfolding and degradation machineHandcuffing reversal is facilitated by proteases and replication initiator monomers.An essential protease involved in bacterial cell-cycle control.Overlapping recognition determinants within the ssrA degradation tag allow modulation of proteolysis.A broad host range replicon with different requirements for replication initiation in three bacterial species.Common domains in the initiators of DNA replication in Bacteria, Archaea and Eukarya: combined structural, functional and phylogenetic perspectives.Protein binding and unfolding by the chaperone ClpA and degradation by the protease ClpAP.Roles of long and short replication initiation proteins in the fate of IncP-1 plasmids.Plasmid replication initiator interactions with origin 13-mers and polymerase subunits contribute to strand-specific replisome assemblyLon and Clp family proteases and chaperones share homologous substrate-recognition domains.The role of the ClpA chaperone in proteolysis by ClpAPPlasmid R6K replication controlThe DnaK-DnaJ-GrpE chaperone system activates inert wild type pi initiator protein of R6K into a form active in replication initiation.Biochemical investigations of control of replication initiation of plasmid R6K.Mechanism and stoichiometry of interaction of DnaG primase with DnaB helicase of Escherichia coli in RNA primer synthesis.Reconstitution of R6K DNA replication in vitro using 22 purified proteins.Redox potential regulates binding of universal minicircle sequence binding protein at the kinetoplast DNA replication origin.Identification of a novel membrane-associated gene product that suppresses toxicity of a TrfA peptide from plasmid RK2 and its relationship to the DnaA host initiation protein.Evolved plasmid-host interactions reduce plasmid interference cost.Opposing effects of DNA on proteolysis of a replication initiator.Conformation of a plasmid replication initiator protein affects its proteolysis by ClpXP system.Protein domains and conformational changes in the activation of RepA, a DNA replication initiator.ParE toxin encoded by the broad-host-range plasmid RK2 is an inhibitor of Escherichia coli gyrase.Structural changes in RepA, a plasmid replication initiator, upon binding to origin DNA.Mutations conferring amino acid residue substitutions in the carboxy-terminal domain of RNA polymerase alpha can suppress clpX and clpP with respect to developmentally regulated transcription in Bacillus subtilis.Plasmid P1 RepA is homologous to the F plasmid RepE class of initiators.Cooperative action of Escherichia coli ClpB protein and DnaK chaperone in the activation of a replication initiation protein.
P2860
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P2860
The replication initiation protein of the broad-host-range plasmid RK2 is activated by the ClpX chaperone.
description
1997 nî lūn-bûn
@nan
1997年の論文
@ja
1997年論文
@yue
1997年論文
@zh-hant
1997年論文
@zh-hk
1997年論文
@zh-mo
1997年論文
@zh-tw
1997年论文
@wuu
1997年论文
@zh
1997年论文
@zh-cn
name
The replication initiation pro ...... tivated by the ClpX chaperone.
@ast
The replication initiation pro ...... tivated by the ClpX chaperone.
@en
type
label
The replication initiation pro ...... tivated by the ClpX chaperone.
@ast
The replication initiation pro ...... tivated by the ClpX chaperone.
@en
prefLabel
The replication initiation pro ...... tivated by the ClpX chaperone.
@ast
The replication initiation pro ...... tivated by the ClpX chaperone.
@en
P2860
P356
P1476
The replication initiation pro ...... tivated by the ClpX chaperone.
@en
P2093
D R Helinski
I Konieczny
P2860
P304
14378-14382
P356
10.1073/PNAS.94.26.14378
P407
P577
1997-12-01T00:00:00Z