Journal
APIDOLOGIE
Volume 53, Issue 1, Pages -Publisher
SPRINGER FRANCE
DOI: 10.1007/s13592-022-00914-9
Keywords
Vitellogenin; nuclear protein; DNA binding
Categories
Funding
- Academy of Finland [265971]
- Natural Sciences and Engineering Research Council of Canada [376088068]
- School of Life Sciences Research Training Initiative at Arizona State University [LM5 1079_GH]
- Research Council of Norway [262137]
- Academy of Finland (AKA) [265971, 265971] Funding Source: Academy of Finland (AKA)
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This study demonstrates that a structural subunit of honey bee Vitellogenin (Vg) can translocate into cell nuclei and bind with DNA. Chromatin immunoprecipitation with sequencing (ChIP-seq) reveals binding sites of Vg at genes influencing immunity and behavior. These findings suggest a new fundamental regulatory role for Vg in the nucleus.
Vitellogenin (Vg) is a conserved protein used by nearly all oviparous animals to produce eggs. It is also pleiotropic and performs functions in oxidative stress resistance, immunity, and, in honey bees, behavioral development of the worker caste. It has remained enigmatic how Vg affects multiple traits. Here, we asked whether Vg enters the nucleus and acts via DNA-binding. We used cell fractionation, immunohistology, and cell culture to show that a structural subunit of honey bee Vg translocates into cell nuclei. We then demonstrated Vg-DNA binding theoretically and empirically with prediction software and chromatin immunoprecipitation with sequencing (ChIP-seq), finding binding sites at genes influencing immunity and behavior. Finally, we investigated the immunological and enzymatic conditions affecting Vg cleavage and nuclear translocation and constructed a 3D structural model. Our data are the first to show Vg in the nucleus and suggest a new fundamental regulatory role for this ubiquitous protein.
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