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Related Experiment Video

Updated: Sep 7, 2025

Homemade Site Directed Mutagenesis of Whole Plasmids

Homemade Site Directed Mutagenesis of Whole Plasmids

Published on: May 11, 2009

Host cell RecA activates a mobile element-encoded mutagenic DNA polymerase.

Debika Ojha¹, Malgorzata M Jaszczur¹, Adhirath Sikand²

¹Department of Biological Sciences, University of Southern California, Los Angeles, CA 90089, USA.

Nucleic Acids Research

|June 23, 2022

Summary

This summary is machine-generated.

Mobile element-encoded DNA polymerase V (pol V) requires host RecA protein to form a functional mutasome complex. This interaction influences polymerase activity and mutagenesis rates, potentially driving bacterial adaptation and antibiotic resistance.

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Area of Science:

Microbiology
Molecular Biology
Genetics

Background:

Homologs of mutagenic Escherichia coli DNA polymerase V (pol V) are found in pathogens and mobile genetic elements.
Mobile element-encoded polymerases (MEPols) can transfer between species, raising questions about their functional requirements in new hosts.

Purpose of the Study:

To investigate the functional requirements of Rum pol (RumA'2B), a model MEPol from the integrative conjugative element R391.
To determine if Rum pol requires host factors for its biochemical activity and mutagenic potential.

Main Methods:

Biochemical assays were used to study the activity of Rum pol in vitro.
Mutagenesis rates were measured in vivo in recipient bacteria.
The role of RecA protein from various bacterial hosts was investigated.

Main Results:

Rum pol biochemical activity necessitates the formation of a mutasomal complex (Rum Mut) involving RumA'2B, RecA, and ATP.
RecA protein is supplied by the recipient bacterium.
The specific activity of Rum Mut and in vivo mutagenesis rates are influenced by the phylogenetic distance between host RecA and E. coli RecA.

Conclusions:

Rum pol functions as a mobile catalyst of evolution, requiring host RecA for activity.
The dependence on host RecA suggests a mechanism for adapting to diverse bacterial environments.
This mobile polymerase can generate a broad mutational landscape, potentially facilitating bacterial adaptation and the emergence of antibiotic resistance.