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@article{2211224, author = {Kolesár, Peter and Stejskal, Karel and Potěšil, David and Murray, Johanne M and Paleček, Jan}, article_location = {BASEL}, article_number = {1}, doi = {http://dx.doi.org/10.3390/cells11010165}, keywords = {SMC5; 6; Nse1; ubiquitin ligase; ubiquitination; Ubc13; Mms2; Nse4 kleisin}, language = {eng}, issn = {2073-4409}, journal = {Cells}, title = {Role of Nse1 Subunit of SMC5/6 Complex as a Ubiquitin Ligase}, url = {https://www.mdpi.com/2073-4409/11/1/165}, volume = {11}, year = {2022} }
TY - JOUR ID - 2211224 AU - Kolesár, Peter - Stejskal, Karel - Potěšil, David - Murray, Johanne M - Paleček, Jan PY - 2022 TI - Role of Nse1 Subunit of SMC5/6 Complex as a Ubiquitin Ligase JF - Cells VL - 11 IS - 1 SP - 1-13 EP - 1-13 PB - MDPI SN - 20734409 KW - SMC5 KW - 6 KW - Nse1 KW - ubiquitin ligase KW - ubiquitination KW - Ubc13 KW - Mms2 KW - Nse4 kleisin UR - https://www.mdpi.com/2073-4409/11/1/165 N2 - Structural Maintenance of Chromosomes (SMC) complexes are important for many aspects of the chromosomal organization. Unlike cohesin and condensin, the SMC5/6 complex contains a variant RING domain carried by its Nse1 subunit. RING domains are characteristic for ubiquitin ligases, and human NSE1 has been shown to possess ubiquitin-ligase activity in vitro. However, other studies were unable to show such activity. Here, we confirm Nse1 ubiquitin-ligase activity using purified Schizosaccharomyces pombe proteins. We demonstrate that the Nse1 ligase activity is stimulated by Nse3 and Nse4. We show that Nse1 specifically utilizes Ubc13/Mms2 E2 enzyme and interacts directly with ubiquitin. We identify the Nse1 mutation (R188E) that specifically disrupts its E3 activity and demonstrate that the Nse1-dependent ubiquitination is particularly important under replication stress. Moreover, we determine Nse4 (lysine K181) as the first known SMC5/6-associated Nse1 substrate. Interestingly, abolition of Nse4 modification at K181 leads to suppression of DNA-damage sensitivity of other SMC5/6 mutants. Altogether, this study brings new evidence for Nse1 ubiquitin ligase activity, significantly advancing our understanding of this enigmatic SMC5/6 function. ER -
KOLESÁR, Peter, Karel STEJSKAL, David POTĚŠIL, Johanne M MURRAY a Jan PALEČEK. Role of Nse1 Subunit of SMC5/6 Complex as a Ubiquitin Ligase. \textit{Cells}. BASEL: MDPI, 2022, roč.~11, č.~1, s.~1-13. ISSN~2073-4409. Dostupné z: https://dx.doi.org/10.3390/cells11010165.
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