Characterization of the NSE6 subunit of the Physcomitrium patens SMC5/6 complex
| Autoři | |
|---|---|
| Rok publikování | 2022 |
| Druh | Konferenční abstrakty |
| Fakulta / Pracoviště MU | |
| Citace | |
| Popis | Structural Maintenance of Chromosome (SMC) complexes are molecular machines ensuring chromatin organization at higher levels. They play direct roles in cohesion, condensation, replication, transcription and DNA repair. Their cores are composed of long-armed SMC, kleisin, and kleisin-associated KITE or HAWK subunits. Additional NSE5 and NSE6 regulatory subunits interact with both SMC5 and SMC6 arms. Although their amino acid sequences are poorly conserved across the species, their primary function is to target SMC5/6 to the DNA damage sites. To characterize the NSE6 subunit of moss Physcomitrium patens, we analyzed its protein-protein interactions and Ppnse6 mutant phenotypes. In the human HsNSE6, we recently identified a new CANIN (for Coiled-coil SMC6 And NSE5 INteracting) domain. To further explore the conservation of this domain, we tracked down its sequence homology to lower plants and characterized its most conserved motif required for binding to its NSE5 partner. In addition, the CANIN domain and its preceding sequences bind and link SMC5 and SMC6 arms, suggesting its role in SMC5/6 dynamics. We hypothesized that this bridging of SMC5-SMC6 arms might negatively impact their dynamics, e.g. by limiting the opening of the SMC5/6 ring upon ATP binding. |
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