Analysis of the interaction of histone-H-NS motif-containing proteins with the bacterial genetic material

Abstract

The investigation of global regulatory proteins of gene expression represents a significant advance in the understanding of the regulation of critical processes in pathogenic microorganisms. Among these proteins, the histone-like nucleoid structuring protein (H-NS) is found in several bacteria, mainly playing a role as a transcriptional repressor. H-NS has been extensively characterized in a few bacteria, such as Escherichia coli and Salmonella enterica. Strikingly, Bartonella henselae and Burkholderia cenocepacia encode atypical proteins with the histone_H-NS motif. In B. henselae, the shortened H-NS protein plays a crucial role in silencing genes of the type IV secretion system, which are decisive for the entry of the bacterium into erythrocytes during the infection process. However, the complete set of genes regulated by this protein remains to be determined. In B. cenocepacia, an atypically large hypothetical protein with the histone_H-NS motif was identified, whose DNA-binding function has not yet been characterized. To explore the DNA-binding function of these two atypical proteins and understand their role in gene expression regulation, we aim to determine the binding sites of these proteins in the nucleoid of the respective bacteria. It is important to emphasize that B. henselae and B. cenocepacia are of clinical relevance in Brazil and may represent potential risk of death for patients, especially those who are immunosuppressed or have the genetic disorder condition known as cystic fibrosis