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A Hand-Off Mechanism for Primosome Assembly in Replication Restart

A Hand-Off Mechanism for Primosome Assembly in Replication Restart

http://www.wikidata.org/entity/Q27646355

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Structural insight into the DNA-binding mode of the primosomal proteins PriA, PriB, and DnaT Small-molecule tools for dissecting the roles of SSB/protein interactions in genome maintenance The crystal structure of Neisseria gonorrhoeae PriB reveals mechanistic differences among bacterial DNA replication restart pathways Dimeric structure of the N-terminal domain of PriB protein fromThermoanaerobacter tengcongensissolvedab initio Structural mechanisms of PriA-mediated DNA replication restart Crystal structure of DnaT 84–153 -dT10 ssDNA complex reveals a novel single-stranded DNA binding mode Structure and mechanism of the primosome protein DnaT-functional structures for homotrimerization, dissociation of ssDNA from the PriB·ssDNA complex, and formation of the DnaT·ssDNA complex A bacterial PriB with weak single-stranded DNA binding activity can stimulate the DNA unwinding activity of its cognate PriA helicase The priB gene of Klebsiella pneumoniae encodes a 104-amino acid protein that is similar in structure and function to Escherichia coli PriB.DNA-binding properties of T4 UvsY recombination mediator protein: polynucleotide wrapping promotes high-affinity binding to single-stranded DNA.Recombination and replication.Mealybugs nested endosymbiosis: going into the 'matryoshka' system in Planococcus citri in depth.Genes required for growth at high hydrostatic pressure in Escherichia coli K-12 identified by genome-wide screening.Identification of Subunit Binding Positions on a Model Fork and Displacements That Occur during Sequential Assembly of the Escherichia coli Primosome.Deinococcus radiodurans PriA is a Pseudohelicase Architecture and conservation of the bacterial DNA replication machinery, an underexploited drug target.RecG Directs DNA Synthesis during Double-Strand Break Repair.Genetic method to analyze essential genes of Escherichia coli The PriA replication restart protein blocks replicase access prior to helicase assembly and directs template specificity through its ATPase activity.PriC-mediated DNA replication restart requires PriC complex formation with the single-stranded DNA-binding protein.Functional complementation of UvsX and UvsY mutations in the mediation of T4 homologous recombination.A High-Throughput Screening Strategy to Identify Protein-Protein Interaction Inhibitors That Block the Fanconi Anemia DNA Repair Pathway.Multiple C-terminal tails within a single E. coli SSB homotetramer coordinate DNA replication and repair.An SOS inhibitor that binds to free RecA protein: the PsiB protein.An aromatic-rich loop couples DNA binding and ATP hydrolysis in the PriA DNA helicase.Recruitment to stalled replication forks of the PriA DNA helicase and replisome-loading activities is essential for survival.A Replisome's journey through the bacterial chromosome.Replication Restart in Bacteria.Structure and Function of the PriC DNA Replication Restart Protein.Interactions of the Escherichia coli primosomal PriB protein with the single-stranded DNA. Stoichiometries, intrinsic affinities, cooperativities, and base specificities.Overexpression of the Replicative Helicase in Escherichia coli Inhibits Replication Initiation and Replication Fork Reloading.Modulation of DNA damage tolerance in Escherichia coli recG and ruv strains by mutations affecting PriB, the ribosome and RNA polymerase.A priA Mutant Expressed in Two Pieces Has Almost Full Activity in Escherichia coli K-12.The multi-targeted effects of Chrysanthemum herb extract against Escherichia coli O157:H7.Domain separation and characterization of PriC, a replication restart primosome factor in Escherichia coli.DnaT is a single-stranded DNA binding protein.Mechanisms of bacterial DNA replication restart.Yeast two-hybrid analysis of PriB-interacting proteins in replication restart primosome: a proposed PriB-SSB interaction model.Structural analyses of the bacterial primosomal protein DnaB reveal that it is a tetramer and forms a complex with a primosomal re-initiation protein.Basic and aromatic residues in the C-terminal domain of PriC are involved in ssDNA and SSB binding.

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A Hand-Off Mechanism for Primosome Assembly in Replication Restart

http://www.wikidata.org/entity/Q27646355

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2007 nî lūn-bûn

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2007 թուականի Յունիսին հրատարակուած գիտական յօդուած

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2007 թվականի հունիսին հրատարակված գիտական հոդված

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2007年の論文

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2007年論文

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2007年論文

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2007年論文

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2007年論文

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2007年論文

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2007年论文

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A Hand-Off Mechanism for Primosome Assembly in Replication Restart

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A Hand-Off Mechanism for Primosome Assembly in Replication Restart

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A Hand-Off Mechanism for Primosome Assembly in Replication Restart

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A Hand-Off Mechanism for Primosome Assembly in Replication Restart

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A Hand-Off Mechanism for Primosome Assembly in Replication Restart

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A Hand-Off Mechanism for Primosome Assembly in Replication Restart

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A Hand-Off Mechanism for Primosome Assembly in Replication Restart

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A Hand-Off Mechanism for Primosome Assembly in Replication Restart

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A hand-off mechanism for primosome assembly in replication restart

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Matthew Lopper

http://www.w3.org/2001/XMLSchema#string

Ruethairat Boonsombat

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Steven J Sandler

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P2860

Structure of the DNA binding domain of E. coli SSB bound to ssDNA

Replisome assembly and the direct restart of stalled replication forks

The importance of repairing stalled replication forks

Escherichia coli replication factor Y, a component of the primosome, can act as a DNA helicase

Recombinational DNA repair of damaged replication forks in Escherichia coli: questions.

Multiple genetic pathways for restarting DNA replication forks in Escherichia coli K-12.

Complexed crystal structure of replication restart primosome protein PriB reveals a novel single-stranded DNA-binding mode.

Conversion of phiX174 viral DNA to double-stranded form by purified Escherichia coli proteins.

Structural mechanisms of DNA replication, repair, and recombination.

PriB stimulates PriA helicase via an interaction with single-stranded DNA.

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