Dynamic coupling between the motors of DNA replication: hexameric helicase, DNA polymerase, and primase - Wikidata - awgldk - TriplyDB

Dynamic coupling between the motors of DNA replication: hexameric helicase, DNA polymerase, and primase

Dynamic coupling between the motors of DNA replication: hexameric helicase, DNA polymerase, and primase

http://www.wikidata.org/entity/Q26998987

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Structural insight into the DNA-binding mode of the primosomal proteins PriA, PriB, and DnaT Methods to study the coupling between replicative helicase and leading-strand DNA polymerase at the replication fork The DNA helicase-primase complex as a target for herpes viral infection Mechanism for priming DNA synthesis by yeast DNA Polymerase α Insights into Eukaryotic Primer Synthesis from Structures of the p48 Subunit of Human DNA Primase Structural Basis for the Interaction of a Hexameric Replicative Helicase with the Regulatory Subunit of Human DNA Polymerase -Primase Helicase loading at chromosomal origins of replication Human Primpol1: a novel guardian of stalled replication forks Mechanical operation and intersubunit coordination of ring-shaped molecular motors: insights from single-molecule studies RISC-interacting clearing 3'- 5' exoribonucleases (RICEs) degrade uridylated cleavage fragments to maintain functional RISC in Arabidopsis thaliana.DNA polymerization-independent functions of DNA polymerase epsilon in assembly and progression of the replisome in fission yeast Conformation effects of CpG methylation on single-stranded DNA oligonucleotides: analysis of the opioid peptide dynorphin-coding sequences CMG helicase and DNA polymerase ε form a functional 15-subunit holoenzyme for eukaryotic leading-strand DNA replication.The mini-chromosome maintenance (Mcm) complexes interact with DNA polymerase α-primase and stimulate its ability to synthesize RNA primers Recombinase and translesion DNA polymerase decrease the speed of replication fork progression during the DNA damage response in Escherichia coli cells.Energy-independent helicase activity of a viral genome packaging motor Cooperative base pair melting by helicase and polymerase positioned one nucleotide from each other.Two mechanisms coordinate replication termination by the Escherichia coli Tus-Ter complex.Fine tuning of a DNA fork by the RecQ helicase.DnaC traps DnaB as an open ring and remodels the domain that binds primase.The enzymology of a viral genome packaging motor is influenced by the assembly state of the motor subunits.Strong subunit coordination drives a powerful viral DNA packaging motor.Discrete interactions between bacteriophage T7 primase-helicase and DNA polymerase drive the formation of a priming complex containing two copies of DNA polymerase.Exonuclease of human DNA polymerase gamma disengages its strand displacement function.Watching DNA breath one molecule at a time Regulation of Rad6/Rad18 Activity During DNA Damage Tolerance.DNA substrate recognition and processing by the full-length human UPF1 helicase.Overcoming a nucleosomal barrier to replication.Helicase and polymerase move together close to the fork junction and copy DNA in one-nucleotide steps.Phosphoinositide 3-kinase beta controls replication factor C assembly and function.A mechanistic study of helicases with magnetic traps.Eukaryotic Translesion DNA Synthesis on the Leading and Lagging Strands: Unique Detours around the Same Obstacle Functional interplay of DnaE polymerase, DnaG primase and DnaC helicase within a ternary complex, and primase to polymerase hand-off during lagging strand DNA replication in Bacillus subtilis.DnaT is a single-stranded DNA binding protein.Yeast two-hybrid analysis of PriB-interacting proteins in replication restart primosome: a proposed PriB-SSB interaction model.Hybrid Methods Reveal Multiple Flexibly Linked DNA Polymerases within the Bacteriophage T7 Replisome.A single-molecule approach to DNA replication in Escherichia coli cells demonstrated that DNA polymerase III is a major determinant of fork speed.

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P2860

Dynamic coupling between the motors of DNA replication: hexameric helicase, DNA polymerase, and primase

http://www.wikidata.org/entity/Q26998987

description

2011 nî lūn-bûn

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2011 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած

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2011 թվականի հոտեմբերին 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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2011年論文

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2011年論文

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2011年論文

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2011年论文

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Dynamic coupling between the m ...... e, DNA polymerase, and primase

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Dynamic coupling between the m ...... e, DNA polymerase, and primase

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Dynamic coupling between the m ...... e, DNA polymerase, and primase

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Dynamic coupling between the m ...... e, DNA polymerase, and primase

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Dynamic coupling between the m ...... e, DNA polymerase, and primase

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Dynamic coupling between the m ...... e, DNA polymerase, and primase

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Dynamic coupling between the m ...... e, DNA polymerase, and primase

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Dynamic coupling between the m ...... e, DNA polymerase, and primase

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J.CBPA.2011.08.003

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Current Opinion in Chemical Biology

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Dynamic coupling between the m ...... e, DNA polymerase, and primase

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Divya Nandakumar

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Manjula Pandey

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Smita S Patel

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P2860

Reconstitution of a minimal mtDNA replisome in vitro

SF1 and SF2 helicases: family matters

Single-molecule studies reveal dynamics of DNA unwinding by the ring-shaped T7 helicase

Real-time observation of bacteriophage T4 gp41 helicase reveals an unwinding mechanism

Crystal structure of the helicase domain from the replicative helicase-primase of bacteriophage T7

Crystal structure of T7 gene 4 ring helicase indicates a mechanism for sequential hydrolysis of nucleotides

The structure of a DnaB-family replicative helicase and its interactions with primase

Identification of a DNA primase template tracking site redefines the geometry of primer synthesis

Running in Reverse: The Structural Basis for Translocation Polarity in Hexameric Helicases

Mcm4,6,7 uses a "pump in ring" mechanism to unwind DNA by steric exclusion and actively translocate along a duplex.

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595-605

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10.1016/J.CBPA.2011.08.003

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21865075

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