PDF(Pubmed)
Abstract：
RecA ATPases are a family of proteins that catalyzes the exchange of complementary DNA regions via homologous recombination. They are conserved from bacteria to humans and are crucial for DNA damage repair and genetic diversity. In this work, Knadler et al. examine how ATP hydrolysis and divalent cations impact the recombinase activity of Saccharolobus solfataricus RadA protein (ssoRadA). They find that the ssoRadA-mediated strand exchange depends on ATPase activity. The presence of Manganese reduces ATPase activity and enhances strand exchange, while calcium inhibits ATPase activity by preventing ATP binding to the protein, yet destabilizes the nucleoprotein ssoRadA filaments, allowing strand exchange regardless of the ATPase activity. Although RecA ATPases are highly conserved, this research offers intriguing new evidence that each member of the family requires individual evaluation.
摘要：
RecAATP酶是通过同源重组催化互补DNA区域交换的蛋白质家族。它们从细菌到人类都是保守的，对于DNA损伤修复和遗传多样性至关重要。在这项工作中,Knadler等人。检查ATP水解和二价阳离子如何影响蔗糖RadA蛋白（ssoRadA）的重组酶活性（1）。他们发现ssoRadA介导的链交换取决于ATPase活性。锰的存在降低ATPase活性并增强链交换，钙通过阻止ATP与蛋白质结合来抑制ATP酶活性，然而却使核蛋白ssoRadA细丝不稳定，允许链交换而不管ATP酶活性。虽然RecAATP酶是高度保守的，这项研究提供了有趣的新证据，即每个家庭成员都需要单独评估。
