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@article{1662637,
author = {Vondrová, Lucie and Kolesár, Peter and Adamus, Marek and Nociar, Matej and Oliver, Antony William and Paleček, Jan},
article_location = {London},
article_number = {1},
doi = {http://dx.doi.org/10.1038/s41598-020-66647-w},
keywords = {Biochemistry; Genetics; Molecular biology; Structural biology},
language = {eng},
issn = {2045-2322},
journal = {Scientific reports},
title = {A role of the Nse4 kleisin and Nse1/Nse3 KITE subunits in the ATPase cycle of SMC5/6},
url = {https://doi.org/10.1038/s41598-020-66647-w},
volume = {10},
year = {2020}
}
TY - JOUR
ID - 1662637
AU - Vondrová, Lucie - Kolesár, Peter - Adamus, Marek - Nociar, Matej - Oliver, Antony William - Paleček, Jan
PY - 2020
TI - A role of the Nse4 kleisin and Nse1/Nse3 KITE subunits in the ATPase cycle of SMC5/6
JF - Scientific reports
VL - 10
IS - 1
SP - 1-13
EP - 1-13
PB - Nature Publishing Group
SN - 20452322
KW - Biochemistry
KW - Genetics
KW - Molecular biology
KW - Structural biology
UR - https://doi.org/10.1038/s41598-020-66647-w
L2 - https://doi.org/10.1038/s41598-020-66647-w
N2 - The SMC (Structural Maintenance of Chromosomes) complexes are composed of SMC dimers, kleisin and kleisin-interacting (HAWK or KITE) subunits. Mutual interactions of these subunits constitute the basal architecture of the SMC complexes. In addition, binding of ATP molecules to the SMC subunits and their hydrolysis drive dynamics of these complexes. Here, we developed new systems to follow the interactions between SMC5/6 subunits and the relative stability of the complex. First, we show that the N-terminal domain of the Nse4 kleisin molecule binds to the SMC6 neck and bridges it to the SMC5 head. Second, binding of the Nse1 and Nse3 KITE proteins to the Nse4 linker increased stability of the ATP-free SMC5/6 complex. In contrast, binding of ATP to SMC5/6 containing KITE subunits significantly decreased its stability. Elongation of the Nse4 linker partially suppressed instability of the ATP-bound complex, suggesting that the binding of the KITE proteins to the Nse4 linker constrains its limited size. Our data suggest that the KITE proteins may shape the Nse4 linker to fit the ATP-free complex optimally and to facilitate opening of the complex upon ATP binding. This mechanism suggests an important role of the KITE subunits in the dynamics of the SMC5/6 complexes.
ER -
VONDROVÁ, Lucie, Peter KOLESÁR, Marek ADAMUS, Matej NOCIAR, Antony William OLIVER and Jan PALEČEK. A role of the Nse4 kleisin and Nse1/Nse3 KITE subunits in the ATPase cycle of SMC5/6. \textit{Scientific reports}. London: Nature Publishing Group, vol.~10, No~1, p.~1-13. ISSN~2045-2322. doi:10.1038/s41598-020-66647-w. 2020.
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