Analysis and the identification of DNA binding sites for the cI repressor of Bacteriophage ɛ34

Abstract

Gene 46 of ɛ34 encodes a protein that is similar to other phage repressors. It has a C‐terminal protease domain which is about 80% identical to the repressors of phage λ, but its DNA binding N‐terminal portion is only about 18% identical to its closest known relatives in phages λ, and Lex A. The N‐terminal DNA‐binding domain is homologous to the HTH_XRE family of DNA‐binding domains. In another study we have generated homology models of this proteins and its interaction with DNA [1].The main goal of this project was to initiate a structure‐function study on the cI repressor protein of phage ɛ34. The cI repressor of ɛ34 protein with a 6X polyhistidine tag was first isolated and purified to homogeneity. We have identified regions for cI binding by using bioinformatics and gel‐mobility shift assay using PCR fragments encompassing the intergenic region of the cI and cro gene. Our binding sites compare well with the known intergenic regions of other phages such as λ, Φ11, 434. This project was done as a collaborative venture between two laboratories, Huntingdon College (Dr. Doba Jackson) and Alabama State University (laboratory of Dr. Robert Villafane). This project is in line with Dr. Robert Villafane's research into the Genomic analysis of bacteriophage ɛ34 of Salmonella enteric serovar Anatum.Support or Funding InformationSupport Support for this work was provided by Alabama State University and Huntingdon College.This abstract is from the Experimental Biology 2019 Meeting. There is no full text article associated with this abstract published in The FASEB Journal.