Biochemical Properties and Roles of DprA Protein in Bacterial Natural Transformation, Virulence, and Pilin Variation.

Dhirendra Kumar Sharma, Hari S Misra, Subhash C Bihani, Yogendra S Rajpurohit

Journal: Journal of bacteriology 2023;205(2):e0046522

PMID: 36695594

Abstract

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 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.

Address: Molecular Biology Division, Bhabha Atomic Research Centre, Mumbai, Maharashtra, India.; Homi Bhabha National Institute (DAE-Deemed University), Mumbai, Maharashtra, India.; Radiation Biology & Health Sciences Division, Bhabha Atomic Research Centre, Mumbai, Maharashtra, India.
Bant logo

© Copyright 2026, Nutrition Evidence

NED wishes to thank the following organisations for their support:

We use cookies to improve your experience and analyze site traffic with Google Analytics. By continuing to use our site, you agree to our use of cookies. Learn more.