Regulation mechanism of cAMP Receptor Protein in Low-Molecular-Weight Bacteriocin Secretion by Pectobacterium carotovorum subsp. caratovorum Ruchi Briam James Sersenia Lagitnay 1,2**, Tzu-Rong Li 2, Duen-Yau Chuang 2
1 Natural Sciences Department, College of Arts & Sciences, Nueva Vizcaya State University, Philippines
2 Chemistry Department, College of Sciences, National Chung Hsing University, Taiwan
Abstract
Pectobacterium carotovorum subsp. carotovorum (Pcc) is a phytopathogenic, Gram-negative bacteria. Pcc creates an exotoxin termed bacteriocin, which can kill its gene-related strains, in response to environmental stimuli including nutritional deficiency or UV exposure. The Cyclic AMP receptor protein (CRP), also known as catabolite activator protein (CAP), was the focus of this study as it functions as a regulator of low-molecular-weight bacteriocins (LMWB- carocin). The Pcc crp gene was knocked out via homologous recombination, and the results were examined both in vivo and in vitro. To identify the crp binding sites, a biotinylated probe pull down test was carried out. According to the study^s findings, deletion of the crp gene alters the expression of several low-molecular-weight bacteriocins and suppresses the expression of genes involved in the extracellular export of bacteriocins via the flagellar type three secretion system. In the biotinylated probe pull down assay, crp preferentially binds to one of the two CAP sites when UV induction is absent, however when UV induction is present, crp binds to both of the two CAP sites. In conclusion, our research aimed to simulate the signal transduction system that controls the expression of the carocin gene in response to UV induction.
