Serine Integrase Within the Phage Genome
Student Presenter(s): Roslyn Paul
Faculty Mentor: Bryan Gibb
Department: Biological and Medical Sciences
School/College: College of Arts and Sciences Long Island
Studying bacteriophages can be used for a myriad of reasons, such as phage therapy, phage display, and gene therapy. Bacteriophages throughout many clusters have the gene coding for serine integrase in common. The protein structure for this gene is highly conserved throughout the cluster to ensure that the efficient genetic recombination reaction occurs when a bacteriophage infects its host. Serine integrase essentially facilitates the insertion of viral DNA into the host genome through Site-Specific Recombination (SSR). It recognizes and attaches itself to the attP attachment site, which is located on the viral genome, and the attB attachment site, which is found on the host genome, to initiate this reaction. These attachment sites are only 40-50bps long, and the recombination carried out by serine integrase is largely irreversible unlike its counterpart, tyrosine recombinases. Serine integrase is a very important protein within the genome of a phage, where its presence can determine a lot about a phage’s virulence. Serine integrase allows phage DNA to be inserted into the bacterial genome to start the less virulent stage called the lysogenic stage which can then become lytic, or the more virulent stage, after a mechanical or chemical stressor. Overall, serine integrase is a very important protein in the genome.