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Related Concept Videos

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...
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...
DNA Replication02:40

DNA Replication

DNA replication involves the separation of the two strands of the double helix, with each strand serving as a template from which the new complementary strand is copied.  After replication, each double-stranded DNA includes one parental or “old” strand and one “new” strand. This is known as semiconservative replication. The resulting DNA molecules have the same sequence and are divided equally into the two daughter cells.
Replication in Prokaryotes
DNA replication uses a large number of...
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
Proofreading01:43

Proofreading

Synthesis of new DNA molecules starts when DNA polymerase links nucleotides together in a sequence that is complementary to the template DNA strand. DNA polymerase has a higher affinity for the correct base to ensure fidelity in DNA replication. The DNA polymerase furthermore proofreads 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 EnzymeGenomic DNA is synthesized in...

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Direct Observation of Enzymes Replicating DNA Using a Single-molecule DNA Stretching Assay
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A trimeric DNA polymerase complex increases the native replication processivity.

Andrey L Mikheikin1, Hsiang-Kai Lin, Preeti Mehta

  • 1Department of Chemistry, University of Pittsburgh, Pittsburgh, PA 15260, USA.

Nucleic Acids Research
|September 24, 2009
PubMed
Summary
This summary is machine-generated.

The Sulfolobus solfataricus DNA polymerase (SsoDpo1) forms a trimer on DNA, enhancing DNA synthesis. This trimeric complex significantly boosts DNA synthesis rate and processivity compared to the monomeric form.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Enzymology

Background:

  • DNA polymerases are crucial enzymes for DNA replication and repair across all life forms.
  • The Sulfolobus solfataricus DNA polymerase (SsoDpo1) exhibits high polymerization speed and exonuclease activity for accurate genome replication.

Purpose of the Study:

  • To investigate the quaternary structure of SsoDpo1 and its functional implications.
  • To determine if SsoDpo1 can form complexes and how these complexes affect its enzymatic activity.

Main Methods:

  • Analytical gel filtration
  • Electrophoretic mobility shift assays (EMSAs)
  • Protein chemical crosslinking
  • Isothermal titration calorimetry (ITC)
  • Fluorescence anisotropy

Main Results:

  • SsoDpo1 self-associates to form a stable trimer in the presence of DNA.
  • Binding of SsoDpo1 to DNA is cooperative, with three polymerase molecules binding to a single DNA substrate.
  • The trimeric SsoDpo1 complex demonstrates significantly increased DNA synthesis rate and processivity.

Conclusions:

  • A trimeric DNA polymerase complex of SsoDpo1 exists and is stabilized by DNA.
  • The trimeric form of SsoDpo1 enhances DNA strand synthesis efficiency compared to the monomeric enzyme.