Biochemical Properties and Roles of DprA Protein in Bacterial Natural Transformation, Virulence, and Pilin Variation.
Dhirendra Kumar SharmaHari Sharan MisraSubhash C BihaniYogendra S RajpurohitPublished in: Journal of bacteriology (2023)
Natural transformation enables bacteria to acquire DNA from the environment and contributes to genetic diversity, DNA repair, and nutritional requirements. DNA processing protein A (DprA) receives incoming single-stranded DNA and assists RecA loading for homology-directed natural chromosomal transformation and DNA strand annealing during plasmid transformation. The dprA gene occurs in the genomes of all known bacteria, irrespective of their natural transformation status. The DprA protein has been characterized by its molecular, cellular, biochemical, and biophysical properties in several bacteria. This review summarizes different aspects of DprA biology, collectively describing its biochemical properties, molecular interaction with DNA, and function interaction with bacterial RecA during natural transformation. Furthermore, the roles of DprA in natural transformation, bacterial virulence, and pilin variation are discussed.
Keyphrases
- circulating tumor
- single molecule
- cell free
- dna repair
- escherichia coli
- genetic diversity
- staphylococcus aureus
- nucleic acid
- pseudomonas aeruginosa
- binding protein
- dna damage
- protein protein
- circulating tumor cells
- antimicrobial resistance
- oxidative stress
- gene expression
- genome wide
- dna damage response
- dna methylation
- transcription factor
- genome wide analysis