Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

The Replisome

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 Replisome

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...

DNA Helicases

DNA Helicases

DNA unwinding helicase enzymes are a type of motor protein. Motor proteins can translocate along filaments or polymers using energy generated from ATP hydrolysis. Helicases are involved in all the important cellular processes where DNA unwinding is required, such as DNA replication, repair, recombination, and transcription. They are present in all living organisms, but vary in their structure, function, and mechanism of action. For example, in prokaryotes, DnaB helicase binds and translocates...

Restriction Enzymes

Restriction Enzymes

Restriction enzymes are bacterial enzymes used to cut DNA in a sequence-specific manner. To cleave DNA, they bind to specific palindromic sequences called restriction sites. Such palindromic DNA sequences or inverted repeats are commonly found in regions of functional significance, such as the origin of replication, gene operator sites, and regions containing transcription termination signals.
The host bacteria protect their own genomic DNA from these enzymes by methylating these sites. Some...

Replication in Eukaryotes

Replication in Eukaryotes

Replication in Eukaryotes

Replication in Eukaryotes

In eukaryotic cells, DNA replication is highly conserved and tightly regulated. Multiple linear chromosomes must be duplicated with high fidelity before cell division, so there are many proteins that fulfill specialized roles in the replication process. Replication occurs in three phases: initiation, elongation, and termination, and ends with two complete sets of chromosomes in the nucleus.
Many Proteins Orchestrate Replication at the Origin
Eukaryotic replication follows many of the same...

You might also read

Related Articles

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

Sort by

Same author

Spermidine biosynthesis by hypervirulent <i>Francisella tularensis</i> promotes fitness and salvages adenine.

Journal of bacteriology·2026

Same author

<i>Francisella tularensis</i> universal stress protein contributes to persistence during growth arrest and paraquat-induced superoxide stress.

Journal of bacteriology·2025

Same author

Polyaminated, acetylated and stop codon readthrough of recombinant Francisella tularensis universal stress protein in Escherichia coli.

PloS one·2024

Same author

Mass Spectrometry of Putrescine, Spermidine, and Spermine Covalently Attached to <i>Francisella tularensis</i> Universal Stress Protein and Bovine Albumin.

Biochemistry research international·2024

Same author

The metabolic control of DNA replication: mechanism and function.

Open biology·2023

Same author

A Public Health Laboratory Information System in Support of Health Emergencies: The Nebraska Public Health Laboratory COVID-19 Experience.

Public health reports (Washington, D.C. : 1974)·2023

Search research articles

Related Experiment Video

Updated: Jun 11, 2026

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

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

Published on: October 8, 2019

Class-specific restrictions define primase interactions with DNA template and replicative helicase.

Marilynn A Larson¹, Mark A Griep, Rafael Bressani

¹Department of Pathology and Microbiology, University of Nebraska Medical Center, Omaha, NE 68198-5900, USA. malarson@unmc.edu

Nucleic Acids Research

|July 2, 2010

Summary

Bacterial primase and helicase interactions are crucial for DNA replication. This study reveals how primase template specificity is conserved within bacterial classes, while primase-helicase interactions co-evolve within species.

More Related Videos

Strand-Specific Analysis of Proteins at Replicating DNA Strands by Enrichment and Sequencing of Protein-Associated Nascent DNA Method

Strand-Specific Analysis of Proteins at Replicating DNA Strands by Enrichment and Sequencing of Protein-Associated Nascent DNA Method

Published on: May 2, 2025

In Vitro Directed Evolution of a Restriction Endonuclease with More Stringent Specificity

In Vitro Directed Evolution of a Restriction Endonuclease with More Stringent Specificity

Published on: March 25, 2020

Related Experiment Videos

Last Updated: Jun 11, 2026

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

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

Published on: October 8, 2019

Strand-Specific Analysis of Proteins at Replicating DNA Strands by Enrichment and Sequencing of Protein-Associated Nascent DNA Method

Strand-Specific Analysis of Proteins at Replicating DNA Strands by Enrichment and Sequencing of Protein-Associated Nascent DNA Method

Published on: May 2, 2025

In Vitro Directed Evolution of a Restriction Endonuclease with More Stringent Specificity

In Vitro Directed Evolution of a Restriction Endonuclease with More Stringent Specificity

Published on: March 25, 2020

Area of Science:

Molecular Biology
Genetics
Biochemistry

Background:

Bacterial DNA replication relies on primase to synthesize RNA primers, a process stimulated by replicative helicase.
Understanding primase regulation is key to deciphering DNA replication mechanisms.

Purpose of the Study:

To investigate the mechanisms regulating bacterial primase activity and its interaction with replicative helicase.
To determine the roles of different primase domains in de novo primer synthesis and template recognition.

Main Methods:

Characterization of primase initiation specificity and helicase interactions in Firmicutes and Proteobacteria.
Utilized mutated, truncated, chimeric, and wild-type primases to assess domain contributions.
Analyzed key residues in the zinc-binding domain for template recognition and specificity transfer.

Main Results:

Identified key residues in the primase zinc-binding domain responsible for class-specific trinucleotide recognition, with substitutions transferring specificity.
Provided evidence for in trans interaction between primase domains, influencing template recognition.
Demonstrated species-specific modulation of RNA primer length by helicase binding, correlating with genetic relatedness.

Conclusions:

Bacterial primase template specificity is conserved within bacterial classes.
Primase-helicase interactions have co-evolved within individual bacterial species, highlighting functional adaptation.