In the microbial world, bacterial mutation and the transmission of genetic information are a process full of surprises. Recent studies have revealed the critical role that integrated host factors (IHFs) play in bacterial genomes, particularly in gene transduction using lambda phage. This study not only provides insights into bacterial genetic recombination, but also reveals how these processes can be exploited to develop new microbial technologies.
Integrating host factor is a multifunctional DNA-binding protein that is essential for E. coli and some of its phages.
IHF is a heterodimeric protein mainly encoded by himA and himD genes. Its presence not only promotes bacterial genetic recombination, but also plays an important role in the DNA replication and transcription processes. When IHF binds to specific DNA sequences, it bends the DNA structure, helping cells recognize and regulate gene expression.
When IHF was first discovered, it was only thought to be related to specific phage recombination, but as research deepened, scientists gradually realized that it plays multiple roles in the physiological processes of E. coli, including phage packaging. and distribution, DNA replication, and expression of many genes. This makes IHF an indispensable protein in bacteria, important for DNA replication and gene expression.
A study explored how genetic information is transferred from E. coli to Salmonella cells by lambda phage and observed changes this process caused in the transduction and lysogenic stages of Salmonella progeny. The results showed that in some mutant Salmonella strains, there were no centers or spots of infection.
Studies have shown that lambda phage can effectively transduce the gene of E. coli K-12 into Salmonella.
In this process, E. coli genes are transduced into Salmonella bacteria during the lytic phase through IHF and expressed. These mutant Salmonella strains have an altered lysogenic state in the presence of galactose, resulting in cells that fail to lyse even in the presence of treatments such as meclomycin, UV light, or even heat.
Another study focused on the performance of HU and IHF in different experimental mutant E. coli strains. Both proteins play auxiliary roles in the interaction of bacteriophage lambda. Experiments have found that if both HU and IHF are lacking, the lytic growth of the phage is limited and spots cannot be formed. This shows that at least one of these two proteins is essential for the DNA maturation process.
The structural similarities of HU and IHF make them interchangeable in certain processes, but it has been proven experimentally that they are not completely interchangeable.
For example, IHF is necessary when the phage has a cos site mutation or the host has a DNA gyrase mutation. This means that the interactions between these proteins are important in microbial genetic processes and are crucial for manipulating the transmission of genes.
These findings provide new insights into the mechanisms of gene transfer and allow us to gain a deeper understanding of how bacteria adapt and evolve within their genomes. Through research on lambda phage, we can develop new microbial technologies and even use these bacteria for gene editing and therapy. How do bacteria use these mechanisms to adapt to environmental changes during their evolution?