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Related Concept Videos

Translesion DNA Polymerases02:10

Translesion DNA Polymerases

Translesion (TLS) polymerases rescue stalled DNA polymerases at sites of damaged bases by replacing the replicative polymerase and installing a nucleotide across the damaged site. Doing so, TLS allows additional time for the cell to repair the damage before resuming regular DNA replication.
TLS polymerases are found in all three domains of life - archaea, bacteria, and eukaryotes. Of the different classes of TLS polymerases, members of the Y family are fitted with specialized structures that...
Restarting Stalled Replication Forks02:37

Restarting Stalled Replication Forks

DNA replication is initiated at sites containing predefined DNA sequences known as origins of replication. DNA is unwound at these sites by the minichromosome maintenance (MCM) helicase and other factors such as Cdc45 and the associated GINS complex.The unwound single strands are protected by replication protein A (RPA) until DNA polymerase starts synthesizing DNA at the 5’ end of the strand in the same direction as the replication fork. To prevent the replication fork from falling apart, a...
Homologous Recombination02:31

Homologous Recombination

The basic reaction of homologous recombination (HR) involves two chromatids that contain DNA sequences sharing a significant stretch of identity. One of these sequences uses a strand from another as a template to synthesize DNA in an enzyme-catalyzed reaction. The final product is a novel amalgamation of the two substrates. To ensure an accurate recombination of sequences, HR is restricted to the S and G2 phases of the cell cycle. At these stages, the DNA has been replicated already and the...
The Replisome03:01

The Replisome

DNA replication is carried out by a large complex of proteins that act in a coordinated matter to achieve high-fidelity DNA replication. Together this complex is known as the DNA replication machinery or the replisome.
The synthesis of the leading and lagging strands is a highly coordinated process. To explain this, the “Trombone model” was proposed by Bruce Alberts in 1980. The DNA loop formation starts when a primer is synthesized on the parent lagging strand. The loop grows with the...
The Replisome03:01

The Replisome

DNA replication is carried out by a large complex of proteins that act in a coordinated matter to achieve high-fidelity DNA replication. Together this complex is known as the DNA replication machinery or the replisome.
The synthesis of the leading and lagging strands is a highly coordinated process. To explain this, the “Trombone model” was proposed by Bruce Alberts in 1980. The DNA loop formation starts when a primer is synthesized on the parent lagging strand. The loop grows with the...
Proofreading01:31

Proofreading

Synthesis of new DNA molecules is carried out by the enzyme DNA polymerase, which adds nucleotides on the daughter strand complementary to the template DNA strand. DNA polymerase has a higher affinity to add the correct base and ensures fidelity during DNA replication. Furthermore,  it exhibits proofreading activity during replication, using an exonuclease domain that cuts off incorrect nucleotides from the nascent DNA strand.
Errors During Replication are Corrected by the DNA Polymerase Enzyme

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Analyzing DNA-Protein Interactions with Streptavidin-Based Biolayer Interferometry
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Interaction between DNA Polymerase lambda and RPA during translesion synthesis.

Yu S Krasikova1, E A Belousova, N A Lebedeva

  • 1Institute of Chemical Biology and Fundamental Medicine, Siberian Branch of the Russian Academy of Sciences, Novosibirsk, 630090, Russia.

Biochemistry. Biokhimiia
|November 4, 2008
PubMed
Summary

Replication protein A (RPA) enhances DNA polymerase lambda

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Area of Science:

  • Molecular Biology
  • Biochemistry
  • Genetics

Background:

  • DNA repair mechanisms are crucial for maintaining genomic integrity.
  • Translesion synthesis (TLS) is a specialized DNA repair pathway.
  • Replication protein A (RPA) is a key factor in DNA replication and repair.

Purpose of the Study:

  • To investigate the role of human RPA (hRPA) in DNA polymerase lambda-catalyzed TLS.
  • To determine the influence of specific hRPA domains on TLS activity.

Main Methods:

  • Utilized primer-template DNA substrates mimicking TLS intermediates.
  • Incorporated 8-oxoguanine as a DNA lesion.
  • Assessed TLS activity of DNA polymerase lambda with wild-type and mutant hRPA.

Main Results:

  • hRPA significantly stimulated DNA polymerase lambda's TLS activity.
  • This stimulation was conformation-dependent, requiring RPA's globular form.
  • The p70N and p32C domains of hRPA were essential for this stimulatory effect.

Conclusions:

  • Specific domains of RPA are critical for its interaction with DNA polymerase lambda.
  • RPA's conformation influences its ability to modulate TLS.
  • These findings provide insights into the molecular mechanisms of TLS.