Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Translesion DNA Polymerases02:10

Translesion DNA Polymerases

11.0K
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...
11.0K
Proofreading01:31

Proofreading

8.7K
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...
8.7K
Proofreading01:43

Proofreading

60.1K
Overview
60.1K
The Replisome03:01

The Replisome

38.1K
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...
38.1K
The Replisome03:01

The Replisome

9.8K
9.8K
Bacterial RNA Polymerase00:43

Bacterial RNA Polymerase

32.5K
Unlike eukaryotes, bacteria use a single RNA Polymerase (RNAP) to transcribe all genes. The different subunits of bacterial RNAPhave distinct functions. The multisubunit structure of the bacterial RNAP helps the enzyme to maintain catalytic function, facilitate assembly, interact with DNA and RNA, and self-regulate its activity.
In most genes, the transcription site is a single base present upstream of the coding sequence. Though RNAP is a catalytically efficient enzyme, it does not recognize...
32.5K

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Reply to Roske and Yeeles: Mismatch correction by a replicative polymerase constrained on DNA by a ring.

Proceedings of the National Academy of Sciences of the United States of America·2026
Same author

The <i>E. coli</i> DnaX clamp loader sharply bends DNA to load β-clamp at nicks and small gaps.

bioRxiv : the preprint server for biology·2026
Same author

Molecular determinants of Smc5/6 association with DNA junctions.

Nature communications·2026
Same author

DNA polymerase α-primase can function as a translesion DNA polymerase.

bioRxiv : the preprint server for biology·2025
Same author

The proofreading mechanism of the human leading-strand DNA polymerase ε holoenzyme.

Proceedings of the National Academy of Sciences of the United States of America·2025
Same author

The proofreading mechanism of the human leading strand DNA polymerase ε holoenzyme.

bioRxiv : the preprint server for biology·2025

Related Experiment Video

Updated: Jan 18, 2026

DNA Sequence Recognition by DNA Primase Using High-Throughput Primase Profiling
08:04

DNA Sequence Recognition by DNA Primase Using High-Throughput Primase Profiling

Published on: October 8, 2019

9.1K

DNA polymerase α-primase can function as a translesion DNA polymerase.

Ryan Mayle1, Roxana Georgescu1, Michael E O'Donnell1

  • 1HHMI and The Rockefeller University, New York, NY 10065.

Proceedings of the National Academy of Sciences of the United States of America
|September 10, 2025
PubMed
Summary
This summary is machine-generated.

The DNA polymerase Polα, lacking proofreading, uniquely bypasses damaged DNA template nucleotides during replication. Replication Factor C (RFC) also aids Polδ in bypassing lesions, suggesting novel coordination mechanisms.

Keywords:
DNA polymerase alphaDNA repairDNA replicationDNA translesion bypassprimase

More Related Videos

Kinetics of Lagging-strand DNA Synthesis In Vitro by the Bacteriophage T7 Replication Proteins
08:14

Kinetics of Lagging-strand DNA Synthesis In Vitro by the Bacteriophage T7 Replication Proteins

Published on: February 25, 2017

7.8K
Single-Molecule Fluorescence Visualization of DNA Polymerase Dynamics at G-Quadruplexes
05:37

Single-Molecule Fluorescence Visualization of DNA Polymerase Dynamics at G-Quadruplexes

Published on: April 4, 2025

1.2K

Related Experiment Videos

Last Updated: Jan 18, 2026

DNA Sequence Recognition by DNA Primase Using High-Throughput Primase Profiling
08:04

DNA Sequence Recognition by DNA Primase Using High-Throughput Primase Profiling

Published on: October 8, 2019

9.1K
Kinetics of Lagging-strand DNA Synthesis In Vitro by the Bacteriophage T7 Replication Proteins
08:14

Kinetics of Lagging-strand DNA Synthesis In Vitro by the Bacteriophage T7 Replication Proteins

Published on: February 25, 2017

7.8K
Single-Molecule Fluorescence Visualization of DNA Polymerase Dynamics at G-Quadruplexes
05:37

Single-Molecule Fluorescence Visualization of DNA Polymerase Dynamics at G-Quadruplexes

Published on: April 4, 2025

1.2K

Area of Science:

  • Molecular Biology
  • Genetics
  • Biochemistry

Background:

  • Eukaryotic DNA replication utilizes Polα-primase to create RNA-DNA primers.
  • Polα's DNA polymerase subunit (Pol1) lacks 3'-5' proofreading exonuclease activity.
  • High-fidelity polymerases Polδ and Polε possess proofreading but synthesize the bulk of the genome.

Purpose of the Study:

  • To investigate the functional significance of Polα's lack of proofreading.
  • To understand how Polα handles damaged template nucleotides during replication.
  • To explore the role of Replication Factor C (RFC) in DNA repair and replication bypass.

Main Methods:

  • In vitro biochemical assays to assess polymerase activity.
  • Analysis of Polα's ability to traverse oxidized and hydrolyzed DNA template bases.
  • Investigating the effect of RFC on Polδ-mediated lesion bypass.

Main Results:

  • Polα demonstrates a unique capability to replicate past common oxidized or hydrolyzed template nucleotides.
  • This suggests Polα is specialized for bypassing template lesions during chromosome replication.
  • RFC was found to stimulate Polδ lesion bypass independently of PCNA loading.

Conclusions:

  • Polα's lack of proofreading is an evolutionary adaptation for bypassing template lesions.
  • A novel coordination mechanism between Polδ and RFC, independent of PCNA, may exist for lesion bypass.