Location: Bee Research LaboratoryTitle: A secreted RNA binding protein forms RNA-stabilizing granules in the honeybee royal jelly
|MAORI, EYAL - University Of Cambridge|
|NAVARRO, ISABELA - University Of Cambridge|
|BONCRISTIANI, HUMBERTO - University Of Florida|
|SEILLY, DAVID - Commonwealth Scientific And Industrial Research Organisation (CSIRO)|
|RUDOLPH, KONRAD - University Of Cambridge|
|SAPETSCHING, ALEXANDRA - University Of Cambridge|
|LIN, CHI-CHUAN - University Of Leeds|
|LADBURY, JOHN - University Of Leeds|
|HEENEY, JONATHAN - University Of Cambridge|
Submitted to: Molecular Cell
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: 3/5/2019
Publication Date: 5/2/2019
Citation: Maori, E., Navarro, I., Boncristiani, H., Seilly, D.J., Rudolph, K., Sapetsching, A., Lin, C., Ladbury, J.E., Evans, J.D., Heeney, J. 2019. A secreted RNA binding protein forms RNA-stabilizing granules in the honeybee royal jelly. Molecular Cell. 74(3):598-608.e6. https://doi.org/10.1016/j.molcel.2019.03.010.
Interpretive Summary: Honey bees provision their larvae with royal jelly and worker jelly, secretions produced by nurse worker bees. It has been found that these secretions contain RNA that can affect the health of those feeding on worker jelly. This work describes a protein that helps in this process. The results are novel and have a strong potential impact on bee management and bee disease.
Technical Abstract: RNA flow between organisms has been documented within and among different kingdoms of life. Recently, we demonstrated horizontal RNA transfer between honeybees involving secretion and ingestion of worker and royal jellies. However, how the jelly facilitates transfer of RNA is still unknown. Here, we show that worker and royal jellies harbor robust RNA-binding activity. We report that a highly abundant jelly component, major royal jelly protein 3 (MRJP-3), acts as an extracellular non-sequence-specific RNA-aggregating factor. Multivalent RNA binding stimulates higher-order assembly of MRJP-3 into extracellular ribonucleoprotein granules that protect RNA from degradation and enhance RNA bioavailability. These findings reveal that honeybees have evolved a secreted dietary RNA-binding factor to concentrate, stabilize, and share RNA among individuals. Our work identifies high-order ribonucleoprotein assemblies with functions outside cells and organisms.