The unstructured C-terminus of the tau subunit of Escherichia coli DNA polymerase III holoenzyme is the site of interaction with the alpha subunit
about
Solution structure of Domains IVa and V of the subunit of Escherichia coli DNA polymerase III and interaction with the subunitA novel zinc-binding fold in the helicase interaction domain of the Bacillus subtilis DnaI helicase loaderStructure of the PolIIIα-τc-DNA Complex Suggests an Atomic Model of the ReplisomeThe N-terminal region of the bacterial DNA polymerase PolC features a pair of domains, both distantly related to domain V of the DNA polymerase III τ subunit.Allosteric regulation of the primase (DnaG) activity by the clamp-loader (tau) in vitro.Suppression of isotope scrambling in cell-free protein synthesis by broadband inhibition of PLP enymes for selective 15N-labelling and production of perdeuterated proteins in H2O.Essential biological processes of an emerging pathogen: DNA replication, transcription, and cell division in Acinetobacter sppdnaX36 Mutator of Escherichia coli: effects of the {tau} subunit of the DNA polymerase III holoenzyme on chromosomal DNA replication fidelity.Investigating the predictability of essential genes across distantly related organisms using an integrative approachArchitecture and conservation of the bacterial DNA replication machinery, an underexploited drug target.Plasmid replication initiator interactions with origin 13-mers and polymerase subunits contribute to strand-specific replisome assemblySelective disruption of the DNA polymerase III α-β complex by the umuD gene products.The β2 clamp in the Mycobacterium tuberculosis DNA polymerase III αβ2ε replicase promotes polymerization and reduces exonuclease activity.A direct proofreader-clamp interaction stabilizes the Pol III replicase in the polymerization mode.The proofreading exonuclease subunit epsilon of Escherichia coli DNA polymerase III is tethered to the polymerase subunit alpha via a flexible linker.A single subunit directs the assembly of the Escherichia coli DNA sliding clamp loader.Single-molecule studies of fork dynamics in Escherichia coli DNA replication.Comprehensive mapping of the C-terminus of flap endonuclease-1 reveals distinct interaction sites for five proteins that represent different DNA replication and repair pathwaysPolymerase manager protein UmuD directly regulates Escherichia coli DNA polymerase III α binding to ssDNA.A novel essential domain perspective for exploring gene essentiality.cryo-EM structures of the E. coli replicative DNA polymerase reveal its dynamic interactions with the DNA sliding clamp, exonuclease and τ.Single-molecule visualization of fast polymerase turnover in the bacterial replisome.Genome-Wide Identification and Expression, Protein-Protein Interaction and Evolutionary Analysis of the Seed Plant-Specific BIG GRAIN and BIG GRAIN LIKE Gene Family.Noise in the Machine: Alternative Pathway Sampling is the Rule During DNA Replication.
P2860
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P2860
The unstructured C-terminus of the tau subunit of Escherichia coli DNA polymerase III holoenzyme is the site of interaction with the alpha subunit
description
2007 nî lūn-bûn
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2007年の論文
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2007年論文
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name
The unstructured C-terminus of ...... raction with the alpha subunit
@ast
The unstructured C-terminus of ...... raction with the alpha subunit
@en
type
label
The unstructured C-terminus of ...... raction with the alpha subunit
@ast
The unstructured C-terminus of ...... raction with the alpha subunit
@en
prefLabel
The unstructured C-terminus of ...... raction with the alpha subunit
@ast
The unstructured C-terminus of ...... raction with the alpha subunit
@en
P2093
P2860
P50
P356
P1476
The unstructured C-terminus of ...... raction with the alpha subunit
@en
P2093
Jeffrey A Crowther
Kiyoshi Ozawa
Neal K Williams
Slobodan Jergic
Xun-Cheng Su
P2860
P304
P356
10.1093/NAR/GKM079
P407
P577
2007-03-13T00:00:00Z