Year: 2025
Type: article
Abstract: The DprA ( a.k.a . Smf) protein has emerged as a RecA mediator during natural chromosomal transformation, but its ubiquity suggests a possible role in DNA metabolism beyond natural transformation. We show that Bacillus subtilis dprA increases the frequency of Escherichia coli Hfr conjugation. RecA·ATP binds and cooperatively polymerises in a 50-nucleotide (nt) poly deoxy T (dT) 50 ssDNA to form a dynamic filament with SSB competing for binding, but B. subtilis DprA (DprA Bsu ) counters the inhibitory effects of SSB on RecA·ATP filaments. RecA bound to (dT) 21 is poorly active as dATPase, with DprA Bsu significantly improving RecA dATP hydrolysis. RecA Bsu ·dATP-(dT) 20 complexes were readily formed, while DprA Bsu exerts an allosteric effect on RecA Bsu -(dT) 15 complexes competent for dATP hydrolysis. Combining experimental data with a full-atomic model of the RecA-DprA-ssDNA complex’s spatial structure, we proposed a molecular mechanism for DprA-mediated loading of RecA onto short ssDNA stretches. Our results suggest that steric constraints allow for the participation of only one DNA binding site of the DprA dimer in RecA-mediated dATP hydrolysis.
DOI: 10.3390/ijms26167873
Language: English
Topic: DNA Repair Mechanisms
Subfield: Molecular Biology
Domain: Life Sciences
Open Access status: gold
Estimated APC paid: $3,499
Funders: University of Wisconsin-Madison, Ministerio de Ciencia e Innovación, Russian Science Foundation, Université Paris-Sud, Ministry of Science and Higher Education of the Russian Federation, Consejo Superior de Investigaciones Científicas, European Regional Development Fund, Agencia Estatal de Investigación, Centro Nacional de Biotecnología
Awards: G1500796917, G1841455980, G1855990336, G2051388996, G2262748287, G2309174360, G2516005691, G2585926585, G300979063, G3088153535, G3480869486, G3737963664, G425668148, G430777504, G4897010451, G5080475149, G5421974903, G5849541225, G586857820, G6444257319, G6502131828, G725097212, G7391727506, G7850601480, G79130638, G8303708813, G8964889847
OpenAlex ID: W4413376781