How do RuvABC proteins orchestrate the intricate dance of DNA recombination? This review explores the critical roles of RuvA, RuvB, and RuvC proteins in *Escherichia coli*, essential players in homologous genetic recombination and DNA repair. RuvA and RuvB unite to form a complex that fuels ATP-dependent branch migration of Holliday junctions, a pivotal process in heteroduplex DNA formation. RuvA acts as a specificity factor, guiding RuvB, the motor protein, to the junction. The latest structural studies reveal that RuvA tetramers clamp the junction, holding it in a square-planar configuration. Meanwhile, RuvB hexameric rings drive a novel dual helicase action, pumping DNA through the complex using ATP hydrolysis. RuvC endonuclease resolves the Holliday junction by cleaving two DNA strands. Genetic and biochemical evidence suggests that branch migration and resolution are tightly coordinated through direct protein interactions, possibly via a RuvABC complex. This research illuminates the intricate mechanisms of DNA recombination and repair, providing a foundation for future studies exploring the interplay of these proteins. Understanding these processes is crucial for advancements in genetics and biotechnology.
Published in the Annual Review of Genetics, this review is highly relevant due to the journal's focus on genetics and molecular biology. The review synthesizes current knowledge on the RuvABC proteins and their roles in homologous recombination, addressing a central topic within the journal's scope. By offering a comprehensive overview, it serves the journal's goal of providing in-depth analyses of significant advances in genetics.
| Category | Category Repetition |
|---|---|
| Science: Biology (General) | 152 |
| Science: Biology (General): Genetics | 126 |
| Science: Chemistry: Organic chemistry: Biochemistry | 79 |
| Science: Microbiology | 57 |
| Science: Biology (General): Cytology | 48 |