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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 = {1752-301X},
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 - 1752301X
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~1752-301X. Dostupné z: https://dx.doi.org/10.3390/cells11010165.
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