Homo sapiens Raw sequence reads
Like CRBN and VHL, ZYG11B (Zyg-11 family member B) functions as a substrate receptor within the Cullin 2-RING E3 ubiquitin ligase (CRL2) complex. ZYG11B recognizes substrate proteins featuring N-terminal glycine degrons (Gly/N-degrons), which become highly enriched during apoptosis due to caspase cleavage. This process plays a critical role in protein quality control and the maintenance of protein homeostasis. Given ZYG11B's pivotal role in substrate recognition and protein quality control, identifying novel ligands that specifically target this protein is of great interest. In this study, we employed Cluster Systematic Evolution of Ligands by Exponential Enrichment (SELEX) to identify DNA aptamers that selectively bind CRL2ZYG11B without disrupting its ubiquitin ligase activity. The DNA aptamer library was incubated with ZYG11B in PBS binding buffer for positive selection, while magnetic beads were used for counter-selection. After seven rounds of selection, the enriched DNA pool underwent high-throughput sequencing and affinity verification.