ArticleProceedings of the National Academy of Sciences of the United States of America2012
Structure-function analysis of pneumococcal DprA protein reveals that dimerization is crucial for loading RecA recombinase onto DNA during transformation.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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Who cites it
38 citing papers in PubMed, 75 citations in OpenAlex.
- The molecular mechanisms of the ShosTA system in mediating anti-phage defense.Nucleic acids research · 2026Article
- A tripartite protein complex promotes DNA transport during natural transformation in Firmicutes.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- A Single DNA Binding Site of DprA Dimer Is Required to Facilitate RecA Filament Nucleation.International journal of molecular sciences · 2025Article
- Genome-wide antibiotic-CRISPRi profiling identifies LiaR activation as a strategy to resensitize fluoroquinolone-resistant Streptococcus pneumoniae.Nature communications · 2025Article
- Transient inhibition of cell division in competent pneumococcal cells results from deceleration of the septal peptidoglycan complex.Nature communications · 2025Article
- DprA recruits ComM to facilitate recombination during natural transformation in Gram-negative bacteria.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Article
- Natural transformation-specific DprA coordinate DNA double-strand break repair pathways in heavily irradiatedApplied and environmental microbiology · 2024Article
- DNA Transport through the Dynamic Type IV Secretion System.Infection and immunity · 2023Review
- Article
- The RecA-directed recombination pathway of natural transformation initiates at chromosomal replication forks in the pneumococcus.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Expanding natural transformation to improve beneficial lactic acid bacteria.FEMS microbiology reviews · 2022Article
- The acquisition of clinically relevant amoxicillin resistance in Streptococcus pneumoniae requires ordered horizontal gene transfer of four loci.PLoS pathogens · 2022Article
- Targeting evolution of antibiotic resistance by SOS response inhibition.Computational and structural biotechnology journal · 2021Review
- The alternative sigma factor σeLife · 2020Article
- Structural insight into the length-dependent binding of ssDNA by SP_0782 from Streptococcus pneumoniae, reveals a divergence in the DNA-binding interface of PC4-like proteins.Nucleic acids research · 2020Article
- Natural Transformation inFrontiers in microbiology · 2020Article
- Evolution of the Natural Transformation Protein, ComEC, in Bacteria.Frontiers in microbiology · 2018Article
- DprA from Neisseria meningitidis: properties and role in natural competence for transformation.Microbiology (Reading, England) · 2017Article
- Bacterial RadA is a DnaB-type helicase interacting with RecA to promote bidirectional D-loop extension.Nature communications · 2017Article
Corrections and comments
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Authors and funding
15 authors at 6 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Transformation promotes genome plasticity in bacteria via RecA-driven homologous recombination. In the gram-positive human pathogen Streptococcus pneumoniae, the transformasome a multiprotein complex, internalizes, protects, and processes transforming DNA to generate chromosomal recombinants. Double-stranded DNA is internalized as single strands, onto which the transformation-dedicated DNA processing protein A (DprA) ensures the loading of RecA to form presynaptic filaments. We report that the structure of DprA consists of the association of a sterile alpha motif domain and a Rossmann fold and that DprA forms tail-to-tail dimers. The isolation of DprA self-interaction mutants revealed that dimerization is crucial for the formation of nucleocomplexes in vitro and for genetic transformation. Residues important for DprA-RecA interaction also were identified and mutated, establishing this interaction as equally important for transformation. Positioning of key interaction residues on the DprA structure revealed an overlap of DprA-DprA and DprA-RecA interaction surfaces. We propose a model in which RecA interaction promotes rearrangement or disruption of the DprA dimer, enabling the subsequent nucleation of RecA and its polymerization onto ssDNA.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.