A role of the Nse4 kleisin and Nse1/Nse3 KITE subunits in the
ATPase cycle of SMC5/6

J 2020

A role of the Nse4 kleisin and Nse1/Nse3 KITE subunits in the ATPase cycle of SMC5/6

VONDROVÁ, Lucie, Peter KOLESÁR, Marek ADAMUS, Matej NOCIAR, Antony William OLIVER et. al.

Základní údaje

Originální název

A role of the Nse4 kleisin and Nse1/Nse3 KITE subunits in the ATPase cycle of SMC5/6

Autoři

VONDROVÁ, Lucie (203 Česká republika, domácí), Peter KOLESÁR (703 Slovensko, domácí), Marek ADAMUS (203 Česká republika, domácí), Matej NOCIAR (703 Slovensko, domácí), Antony William OLIVER (826 Velká Británie a Severní Irsko) a Jan PALEČEK (203 Česká republika, garant, domácí)

Vydání

Scientific reports, London, Nature Publishing Group, 2020, 2045-2322

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

10601 Cell biology

Stát vydavatele

Velká Británie a Severní Irsko

Utajení

není předmětem státního či obchodního tajemství

Odkazy

URL

Impakt faktor

Impact factor: 4.379

Kód RIV

RIV/00216224:14310/20:00114183

Organizační jednotka

Přírodovědecká fakulta

DOI

http://dx.doi.org/10.1038/s41598-020-66647-w

UT WoS

000560497400006

Klíčová slova anglicky

Biochemistry; Genetics; Molecular biology; Structural biology

Štítky

rivok

Příznaky

Mezinárodní význam, Recenzováno

Změněno: 15. 12. 2020 19:11, Mgr. Marie Šípková, DiS.

Anotace

V originále

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.

Návaznosti

GA18-02067S, projekt VaV

Název: Úloha Nse1/Nse3/Nse4, E3-ubikvitin ligásy, ve stabilitě genomu

Investor: Grantová agentura ČR, Úloha Nse1/Nse3/Nse4, E3-ubikvitin ligásy, ve stabilitě genomu

LQ1601, projekt VaV

Název: CEITEC 2020 (Akronym: CEITEC2020)

Investor: Ministerstvo školství, mládeže a tělovýchovy ČR, CEITEC 2020

Citovat

VONDROVÁ, Lucie, Peter KOLESÁR, Marek ADAMUS, Matej NOCIAR, Antony William OLIVER a Jan PALEČEK. A role of the Nse4 kleisin and Nse1/Nse3 KITE subunits in the ATPase cycle of SMC5/6. Scientific reports. London: Nature Publishing Group, 2020, roč. 10, č. 1, s. 1-13. ISSN 2045-2322. Dostupné z: https://dx.doi.org/10.1038/s41598-020-66647-w.

@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 a 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, 2020, roč.~10, č.~1, s.~1-13. ISSN~2045-2322. Dostupné z: https://dx.doi.org/10.1038/s41598-020-66647-w.

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