Mechanism of RecO recruitment to DNA by single-stranded DNA binding protein - Test2 - elhamkhani - TriplyDB

Mechanism of RecO recruitment to DNA by single-stranded DNA binding protein

Mechanism of RecO recruitment to DNA by single-stranded DNA binding protein

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RecOR complex including RecR N-N dimer and RecO monomer displays a high affinity for ssDNA Genetic recombination in Bacillus subtilis: a division of labor between two single-strand DNA-binding proteins An 'open' structure of the RecOR complex supports ssDNA binding within the core of the complex Structural mechanisms of PriA-mediated DNA replication restart A Decade of Biochemical and Structural Studies of the DNA Repair Machinery of Deinococcus radiodurans: Major Findings, Functional and Mechanistic Insight and Challenges Protein interactions in genome maintenance as novel antibacterial targets The IDL of E. coli SSB links ssDNA and protein binding by mediating protein-protein interactions.SSB and the RecG DNA helicase: an intimate association to rescue a stalled replication fork.RecO protein initiates DNA recombination and strand annealing through two alternative DNA binding mechanisms.Specificity of binding of single-stranded DNA-binding protein to its target.Addressing the Requirements of High-Sensitivity Single-Molecule Imaging of Low-Copy-Number Proteins in Bacteria.RecO and RecR are necessary for RecA loading in response to DNA damage and replication fork stress.SSB functions as a sliding platform that migrates on DNA via reptation.Dual DNA-binding domains shape the interaction of Brh2 with DNA.Interaction with Single-stranded DNA-binding Protein Stimulates Escherichia coli Ribonuclease HI Enzymatic Activity.DNA repair and genome maintenance in Bacillus subtilis.Imaging and energetics of single SSB-ssDNA molecules reveal intramolecular condensation and insight into RecOR function Stimulation of Escherichia coli DNA damage inducible DNA helicase DinG by the single-stranded DNA binding protein SSB.SSB binds to the RecG and PriA helicases in vivo in the absence of DNA.Force and ATP hydrolysis dependent regulation of RecA nucleoprotein filament by single-stranded DNA binding protein.A dual role for mycobacterial RecO in RecA-dependent homologous recombination and RecA-independent single-strand annealing.Structural basis for DNA 5´-end resection by RecJ.PriC-mediated DNA replication restart requires PriC complex formation with the single-stranded DNA-binding protein.Imaging of DNA and Protein-DNA Complexes with Atomic Force Microscopy.The key residue for SSB-RecO interaction is dispensable for Deinococcus radiodurans DNA repair in vivo.DNA-pairing and annealing processes in homologous recombination and homology-directed repair.Protein-protein and peptide-protein docking and refinement using ATTRACT in CAPRI.Surface shapes and surrounding environment analysis of single- and double-stranded DNA-binding proteins in protein-DNA interface.The helicase-binding domain of Escherichia coli DnaG primase interacts with the highly conserved C-terminal region of single-stranded DNA-binding protein.RecF and RecR Play Critical Roles in the Homologous Recombination and Single-Strand Annealing Pathways of Mycobacteria Escherichia coli RadD Protein Functionally Interacts with the Single-stranded DNA-binding Protein.The Borrelia burgdorferi telomere resolvase, ResT, anneals ssDNA complexed with its cognate ssDNA-binding protein.The Borrelia burgdorferi telomere resolvase, ResT, possesses ATP-dependent DNA unwinding activity.Are the SSB-Interacting Proteins RecO, RecG, PriA and the DnaB-Interacting Protein Rep Bound to Progressing Replication Forks in Escherichia coli?RecQ helicase triggers a binding mode change in the SSB-DNA complex to efficiently initiate DNA unwinding.Deinococcus radiodurans DR1088 is a novel RecF-interacting protein that stimulates single-stranded DNA annealing.ATP-dependent conformational change in ABC-ATPase RecF serves as a switch in DNA repair.Fragment-Based Discovery of Inhibitors of the Bacterial DnaG-SSB Interaction.Sak4 of Phage HK620 Is a RecA Remote Homolog With Single-Strand Annealing Activity Stimulated by Its Cognate SSB Protein.Basic and aromatic residues in the C-terminal domain of PriC are involved in ssDNA and SSB binding.

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Mechanism of RecO recruitment to DNA by single-stranded DNA binding protein

http://www.wikidata.org/entity/Q27667563

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2011 nî lūn-bûn

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2011 թուականի Օգոստոսին հրատարակուած գիտական յօդուած

@hyw

2011 թվականի օգոստոսին հրատարակված գիտական հոդված

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2011年の論文

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2011年論文

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2011年論文

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Mechanism of RecO recruitment to DNA by single-stranded DNA binding protein

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Mechanism of RecO recruitment to DNA by single-stranded DNA binding protein

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Mechanism of RecO recruitment to DNA by single-stranded DNA binding protein

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Mechanism of RecO recruitment to DNA by single-stranded DNA binding protein

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Mechanism of RecO recruitment to DNA by single-stranded DNA binding protein

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Mechanism of RecO recruitment to DNA by single-stranded DNA binding protein

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Mechanism of RecO recruitment to DNA by single-stranded DNA binding protein

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Mechanism of RecO recruitment to DNA by single-stranded DNA binding protein

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Mechanism of RecO recruitment to DNA by single-stranded DNA binding protein

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Mechanism of RecO recruitment to DNA by single-stranded DNA binding protein

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Andrew Tran

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Dmitri Postnov

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Olga Koroleva

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Comparative and evolutionary analysis of the bacterial homologous recombination systems

Purified human BRCA2 stimulates RAD51-mediated recombination

Structure of the single-strand annealing domain of human RAD52 protein

DNA replication meets genetic exchange: chromosomal damage and its repair by homologous recombination

RecFOR and RecOR as distinct RecA loading pathways

The process of displacing the single-stranded DNA-binding protein from single-stranded DNA by RecO and RecR proteins

PHENIX: a comprehensive Python-based system for macromolecular structure solution

Reconstitution of initial steps of dsDNA break repair by the RecF pathway of E. coli

Radioresistance of Deinococcus radiodurans: functions necessary to survive ionizing radiation are also necessary to survive prolonged desiccation

The single-stranded DNA-binding protein of Deinococcus radiodurans

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6305-6314

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1985328

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10.1093/NAR/GKR199

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14

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39

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21504984

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3152348

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