E2 S enzymes are implicated in:
Protein Quality Control: Mediating ubiquitination of misfolded proteins for proteasomal degradation .
Stress Response: Regulating cellular responses to oxidative or thermal stress, as observed in homologous Drosophila E2s .
Chromatin Regulation: Some E2s (e.g., Effete/UbcD1) influence chromatin structure and telomere maintenance , though GA22810’s role here remains unconfirmed.
Cloning: GA22810 coding sequences are inserted into expression vectors (e.g., pET or Baculovirus systems) .
Expression: Optimized in E. coli for soluble protein yield .
Purification: Affinity chromatography (e.g., His-tag systems) followed by gel filtration for homogeneity .
Biochemical Assays: Studying ubiquitination kinetics or E2-E3 interactions.
Drug Discovery: Screening for inhibitors/modulators of UPS pathways .
Structural Biology: X-ray crystallography or cryo-EM to resolve catalytic mechanisms .
Knockdown of homologous E2s (e.g., Drosophila UBE2D/eff) disrupts protein degradation, leading to accumulation of polyubiquitinated aggregates . This suggests GA22810 may similarly regulate proteostasis.
Phylogenetic analysis places Drosophila E2s in clades shared with insects and mammals, underscoring functional conservation . For example:
| Drosophila E2 | Human Homolog | Function |
|---|---|---|
| Effete (UbcD1) | UBE2D1-4 | Stress response, proteostasis |
| Ubc10 | UBE2L3 | Immune signaling |
| E2 S (GA22810) | UBE2S | Cell cycle regulation (inferred) |
Substrate Specificity: GA22810’s interaction partners (E3 ligases) remain unidentified.
In Vivo Roles: Functional studies in D. pseudoobscura are needed to elucidate its contributions to development or disease.
Structural Data: No resolved structures for GA22810 exist; homology modeling could bridge this gap.
KEGG: dpo:Dpse_GA22810
STRING: 7237.FBpp0273064