Eukaryotic cells are sensitive to the amount of histones they contain – having either too few or too many histones can result in cellular defects. As many mechanisms that control histone levels act at the transcriptional level, maintaining an appropriate supply of histones is challenging at transcriptionally inactive developmental stages, such as in early embryos. In their study, Michael Welte and colleagues reveal how the availability of the histone variant H2Av is maintained in Drosophila oocytes. They show that H2Av localises to lipid droplets (LDs) in nurse cells, but requires the histone-LD linker protein Jabba for lipid droplet association. However, quantification of H2Av levels in oocytes with and without Jabba shows that transport of LD-associated H2Av from nurse cells makes only a minor contribution to total H2Av in the oocyte. Instead, the authors demonstrate that H2Av levels decline in mature Jabba−/− oocytes. Partial inhibition of the proteasome restores the levels of H2Av in Jabba−/− oocytes, arguing that Jabba is required to maintain H2Av stability. Because H2Av levels in the oocyte scale with those of Jabba and because they decrease when the Jabba-H2Av interaction is abrogated, the authors propose that Jabba physically protects H2Av from degradation. Together, these findings argue that lipid droplets function as histone sequestration sites during oogenesis that ensure a sufficient histone supply by preventing histone degradation.