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Lagging Strand Synthesis01:59

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During replication, the complementary strands in double-stranded DNA are synthesized at different rates. Replication first begins on the leading strand. Replication starts later, occurs more slowly, and proceeds discontinuously on the lagging strand.
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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.
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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.
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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,...
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Updated: Feb 21, 2026

Kinetics of Lagging-strand DNA Synthesis In Vitro by the Bacteriophage T7 Replication Proteins
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Pausing kinetics dominates strand-displacement polymerization by reverse transcriptase.

Omri Malik1,2, Hadeel Khamis1,3, Sergei Rudnizky1

  • 1Faculty of Biology, Technion-Israel Institute of Technology, Haifa 32000, Israel.

Nucleic Acids Research
|October 4, 2017
PubMed
Summary
This summary is machine-generated.

Murine leukemia virus reverse transcriptase (RT) frequently pauses during DNA synthesis. Enzyme backtracking and dissociation/reinitiation, influenced by DNA duplex strength and template structure, regulate RT activity.

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Area of Science:

  • Molecular Biology
  • Virology
  • Biophysics

Background:

  • Reverse transcriptase (RT) is crucial for viral replication, converting RNA into DNA.
  • RT possesses multiple enzymatic activities, including strand displacement polymerization.

Purpose of the Study:

  • To investigate the dynamics of strand-displacement polymerization by murine leukemia virus RT.
  • To identify factors modulating RT pauses, backtracking, and dissociation.

Main Methods:

  • High-resolution optical tweezers were used to monitor single-molecule RT activity.
  • Analysis of enzyme pauses, backtracking, and recovery dynamics.

Main Results:

  • Strand-displacement polymerization by RT is frequently interrupted by pauses.
  • Pauses correlate with DNA duplex strength, suggesting uncharacterized RT/DNA interactions.
  • Enzyme backtracking and recovery are modulated by DNA duplex strength.
  • Dissociation and reinitiation events are influenced by template structure and nucleocapsid protein.

Conclusions:

  • Conserved structural motifs may play a regulatory role in RT activity.
  • Understanding RT dynamics can inform the development of antiviral inhibitors.