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@article{1662630,
author = {Adamus, Marek and Lelkes, Edit and Potěšil, David and Ganji, Sri Ranjani and Kolesár, Peter and Zábrady, Kateřina and Zdráhal, Zbyněk and Paleček, Jan},
article_location = {London},
article_number = {13},
doi = {http://dx.doi.org/10.1016/j.jmb.2020.04.024},
keywords = {human SMC5/6 complex architecture; SMC5-SMC6 dimer coiled-coil arms; NSE1-NSE3-NSE4 trimer; NSE5-NSE6 dimer; CANIN protein-protein interaction domain; MAGE domain},
language = {eng},
issn = {0022-2836},
journal = {Journal of Molecular Biology},
title = {Molecular insights into the architecture of the human SMC5/6 complex},
url = {https://doi.org/10.1016/j.jmb.2020.04.024},
volume = {432},
year = {2020}
}
TY - JOUR
ID - 1662630
AU - Adamus, Marek - Lelkes, Edit - Potěšil, David - Ganji, Sri Ranjani - Kolesár, Peter - Zábrady, Kateřina - Zdráhal, Zbyněk - Paleček, Jan
PY - 2020
TI - Molecular insights into the architecture of the human SMC5/6 complex
JF - Journal of Molecular Biology
VL - 432
IS - 13
SP - 3820-3837
EP - 3820-3837
PB - Academic Press ltd-Elsevier Science ltd
SN - 00222836
KW - human SMC5/6 complex architecture
KW - SMC5-SMC6 dimer coiled-coil arms
KW - NSE1-NSE3-NSE4 trimer
KW - NSE5-NSE6 dimer
KW - CANIN protein-protein interaction domain
KW - MAGE domain
UR - https://doi.org/10.1016/j.jmb.2020.04.024
L2 - https://doi.org/10.1016/j.jmb.2020.04.024
N2 - A family of Structural Maintenance of Chromosome (SMC) complexes is essential for key cellular processes ensuring proper cohesion, condensation and replication. They share a common SMC-kleisin architecture allowing them to embrace DNA. In SMC5/6, the NSE1 and NSE3 KITE and NSE4 kleisin subunits form a stable subcomplex that binds DNA and regulates essential processes. In addition, NSE5 and NSE6 subunits associate with the core SMC5/6 complex and recruit it to DNA repair sites. The architecture of the SMC5/6 complex is crucial for its proper functioning, and mutations within the human SMC5/6 subunits result in severe syndromes. Therefore, we aimed to analyze interactions within the human SMC5/6 complex and determine its detailed architecture. Firstly, we analyzed different parts of SMC5/6 by crosslinking and MS/MS analysis. Our data suggested domain arrangements of hNSE1-hNSE3 and orientation of hNSE4 within the hNSE1-hNSE3-hNSE4 subcomplex. The crosslinking and electron microscopic analysis of the SMC5/6 core complex showed its rod-like architecture with juxtaposed hSMC5-hSMC6 arms. Additionally, we observed fully or partially opened hSMC5-hSMC6 shapes with the hNSE1-hNSE3-hNSE4 trimer localized in the SMC head domains. To complete mapping of the human SMC5/6 complex architecture, we analyzed positions of hNSE5-hNSE6 at the hSMC5-hSMC6 arms. We showed that hNSE6 binding to hNSE5 and the coiled-coil arm of hSMC6 is mediated by a conserved FAM178 domain, which we therefore renamed CANIN (Coiled-coil SMC6 And NSE5 iNteracting) domain. Interestingly, hNSE6 bound both hSMC5 and hSMC6 arms, suggesting that hNSE6 may lock the arms and regulate the dynamics of the human SMC5/6 complex.
ER -
ADAMUS, Marek, Edit LELKES, David POTĚŠIL, Sri Ranjani GANJI, Peter KOLESÁR, Kateřina ZÁBRADY, Zbyněk ZDRÁHAL a Jan PALEČEK. Molecular insights into the architecture of the human SMC5/6 complex. \textit{Journal of Molecular Biology}. London: Academic Press ltd-Elsevier Science ltd, 2020, roč.~432, č.~13, s.~3820-3837. ISSN~0022-2836. Dostupné z: https://dx.doi.org/10.1016/j.jmb.2020.04.024.
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