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Replication in Prokaryotes

Replication in Prokaryotes

DNA replication has three main steps: initiation, elongation, and termination. Replication in prokaryotes begins when initiator proteins bind to the single origin of replication (ori) on the cell's circular chromosome. Replication then proceeds around the entire circle of the chromosome in each direction from the two replication forks, resulting in two DNA molecules.
Many Proteins Work Together to Replicate the Chromosome
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Replication in Prokaryotes

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The DNA Replication Fork

The DNA Replication Fork

An organism’s genome needs to be duplicated in an efficient and error-free manner for its growth and survival. The replication fork is a Y-shaped active region where two strands of DNA are separated and replicated continuously. The coupling of DNA unzipping and complementary strand synthesis is a characteristic feature of a replication fork. Organisms with small circular DNA, such as E. coli, often have a single origin of replication; therefore, they have only two replication forks, one in...

The DNA Replication Fork

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An organism’s genome needs to be duplicated in an efficient and error-free manner for its growth and survival. The replication fork is a Y-shaped active region where two strands of DNA are separated and replicated continuously. The coupling of DNA unzipping and complementary strand synthesis is a characteristic feature of a replication fork. Organisms with small circular DNA, such as E. coli, often have a single origin of replication; therefore, they have only two replication forks, one in...

Replication in Eukaryotes

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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.
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Related Experiment Video

Updated: Jun 4, 2026

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

Structural insight into Helicobacter pylori DNA replication initiation.

Laurent Terradot¹, Anna Zawilak-Pawlik

¹Macromolecular Crystallography Group ESRF; Grenoble Cedex, France.

|February 18, 2011

Summary

This summary is machine-generated.

The regulator HobA is essential for Helicobacter pylori DNA replication initiation by scaffolding the DnaA initiator protein. HobA

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Last Updated: Jun 4, 2026

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

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Determination of the Optimal Chromosomal Location(s) for a DNA Element in Escherichia coli Using a Novel Transposon-mediated Approach

Determination of the Optimal Chromosomal Location(s) for a DNA Element in Escherichia coli Using a Novel Transposon-mediated Approach

Published on: September 11, 2017

Area of Science:

Microbiology
Molecular Biology
Structural Biology

Background:

Helicobacter pylori is a human pathogen with incompletely understood DNA replication mechanisms.
Initiation of DNA replication is a critical step, involving initiator proteins and regulators.
The regulator HobA and initiator protein DnaA interaction in H. pylori is a key area for study.

Purpose of the Study:

To investigate the molecular mechanisms of DNA replication initiation in Helicobacter pylori.
To elucidate the interaction between the DnaA initiator protein and its regulator HobA.
To determine the structural basis of the DnaA-HobA complex and its functional implications.

Main Methods:

X-ray crystallography to determine the structure of DnaA(I-II) in complex with HobA.
Biochemical experiments to analyze the DnaA-HobA complex stoichiometry and DnaA oligomerization.
Site-directed mutagenesis to assess the functional importance of the HobA-DnaA interface.

Main Results:

The crystal structure reveals that a HobA tetramer accommodates up to four DnaA molecules.
Mutations disrupting HobA-DnaA binding are lethal to H. pylori, highlighting HobA's essential role.
HobA acts as a scaffold, promoting DnaA oligomerization crucial for DNA replication initiation.

Conclusions:

HobA is essential for H. pylori DNA replication by facilitating DnaA oligomerization and open complex formation.
The findings provide a model for HobA-dependent DnaA assembly and DNA unwinding.
This study offers insights into bacterial DNA replication, drawing parallels with Escherichia coli.