RecA protein is a central enzyme in homologous DNA recombination, repair and other forms of DNA metabolism in bacteria. It functions as a flexible helix-shaped filament bound on stretched single-stranded or double-stranded DNA in the presence of ATP. In this work, we present an atomic level model for conformational transitions of the RecA filament. The model describes small movements of the RecA N-terminal domain due to coordinated rotation of main chain dihedral angles of two amino acid residues (Psi/Lys23 and Phi/Gly24), while maintaining unchanged the RecA intersubunit interface. The model is able to reproduce a wide range of observed helix pitches in transitions between compressed and stretched conformations of the RecA filament. Predictions of the model are in agreement with Small Angle Neutron Scattering (SANS) measurements of the filament helix pitch in RecA::ADP-AlF(4) complex at various salt concentrations.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1002/prot.21116 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Repeated ionizing radiation exposure induces TRIP13 expression, conferring radioresistance in lung cancer cells.
Sci Rep
January 2025
Reproductive Biology Laboratory, Centre for Reproductive Medicine, Amsterdam UMC, University of Amsterdam, Amsterdam, 1105AZ, The Netherlands.
Radiation therapy is a common treatment modality for lung cancer, and resistance to radiation can significantly affect treatment outcomes. We recently described that lung cancer cells that express more germ cell cancer genes (GC genes, genes that are usually restricted to the germ line) can repair DNA double-strand breaks more rapidly, show higher rates of proliferation and are more resistant to ionizing radiation than cells that express fewer GC genes. The gene encoding TRIP13 appeared to play a large role in this malignant phenotype.
View Article and Find Full Text PDFDistribution of bacterial DNA repair proteins and their co-occurrence with immune systems.
Cell Rep
January 2025
Laboratory of Biochemistry, Wageningen University, 6708 WE Wageningen, the Netherlands. Electronic address:
Article Synopsis
- Bacteria have various DNA repair mechanisms to keep their genomes intact, but identifying these proteins is tricky due to their similarities.
- A new search strategy helps identify and analyze DNA repair proteins, particularly those involved in RecA-dependent homologous recombination, revealing common proteins like RecA and SSB across many species.
- The study finds that some DNA repair proteins are often found alongside immune system components, suggesting a potential link, but no immune system is entirely dependent on a single DNA repair protein, indicating a complex relationship between these systems in bacteria.
RecA deletion disrupts protein homeostasis, leading to deamidation, oxidation, and impaired glycolysis in .
Appl Environ Microbiol
December 2024
School of Medicine, Nankai University, Tianjin, Tianjin, China.
is a foodborne pathogen linked to severe infections in infants and often associated with contaminated powdered infant formula. The RecA protein, a key player in DNA repair and recombination, also influences bacterial resilience and virulence. This study investigated the impact of deletion on the pathogenicity and environmental stress tolerance of BAA-894.
View Article and Find Full Text PDFAdaptation of E. coli to Ciprofloxacin and Enrofloxacin: Differential Proteomics of the SOS Response and RecA-Independent Mechanisms.
Int J Antimicrob Agents
December 2024
University of Amsterdam, Swammerdam Institute of Life Sciences, Molecular Biology and Microbial Food Safety, Amsterdam, The Netherlands. Electronic address:
Antibiotic resistance is a growing global healthcare challenge, treatment of bacterial infections with fluoroquinolones being no exception. These antibiotics can induce genetic instability through several mechanisms, one of the most significant being the activation of the SOS response. During exposure to sublethal concentration, this stress response increases mutation rates, accelerating resistance evolution.
View Article and Find Full Text PDFGenetic modulation of RNA splicing rescues BRCA2 function in mutant cells.
Life Sci Alliance
March 2025
Faculdade de Medicina da Universidade de Lisboa, Lisboa, Portugal
Variants in the hereditary cancer-associated and genes can alter RNA splicing, producing transcripts that encode internally truncated yet potentially functional proteins. However, few studies have quantitatively analyzed variant-specific splicing isoforms. Here, we investigated cells heterozygous and homozygous for the :c.
View Article and Find Full Text PDFWant AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!