Cargando…
A role of the Nse4 kleisin and Nse1/Nse3 KITE subunits in the ATPase cycle of SMC5/6
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 t...
Autores principales: | , , , , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2020
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7297730/ https://www.ncbi.nlm.nih.gov/pubmed/32546830 http://dx.doi.org/10.1038/s41598-020-66647-w |
_version_ | 1783547067259420672 |
---|---|
author | Vondrova, Lucie Kolesar, Peter Adamus, Marek Nociar, Matej Oliver, Antony W. Palecek, Jan J. |
author_facet | Vondrova, Lucie Kolesar, Peter Adamus, Marek Nociar, Matej Oliver, Antony W. Palecek, Jan J. |
author_sort | Vondrova, Lucie |
collection | PubMed |
description | 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. |
format | Online Article Text |
id | pubmed-7297730 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-72977302020-06-17 A role of the Nse4 kleisin and Nse1/Nse3 KITE subunits in the ATPase cycle of SMC5/6 Vondrova, Lucie Kolesar, Peter Adamus, Marek Nociar, Matej Oliver, Antony W. Palecek, Jan J. Sci Rep Article 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. Nature Publishing Group UK 2020-06-16 /pmc/articles/PMC7297730/ /pubmed/32546830 http://dx.doi.org/10.1038/s41598-020-66647-w Text en © The Author(s) 2020 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/. |
spellingShingle | Article Vondrova, Lucie Kolesar, Peter Adamus, Marek Nociar, Matej Oliver, Antony W. Palecek, Jan J. A role of the Nse4 kleisin and Nse1/Nse3 KITE subunits in the ATPase cycle of SMC5/6 |
title | A role of the Nse4 kleisin and Nse1/Nse3 KITE subunits in the ATPase cycle of SMC5/6 |
title_full | A role of the Nse4 kleisin and Nse1/Nse3 KITE subunits in the ATPase cycle of SMC5/6 |
title_fullStr | A role of the Nse4 kleisin and Nse1/Nse3 KITE subunits in the ATPase cycle of SMC5/6 |
title_full_unstemmed | A role of the Nse4 kleisin and Nse1/Nse3 KITE subunits in the ATPase cycle of SMC5/6 |
title_short | A role of the Nse4 kleisin and Nse1/Nse3 KITE subunits in the ATPase cycle of SMC5/6 |
title_sort | role of the nse4 kleisin and nse1/nse3 kite subunits in the atpase cycle of smc5/6 |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7297730/ https://www.ncbi.nlm.nih.gov/pubmed/32546830 http://dx.doi.org/10.1038/s41598-020-66647-w |
work_keys_str_mv | AT vondrovalucie aroleofthense4kleisinandnse1nse3kitesubunitsintheatpasecycleofsmc56 AT kolesarpeter aroleofthense4kleisinandnse1nse3kitesubunitsintheatpasecycleofsmc56 AT adamusmarek aroleofthense4kleisinandnse1nse3kitesubunitsintheatpasecycleofsmc56 AT nociarmatej aroleofthense4kleisinandnse1nse3kitesubunitsintheatpasecycleofsmc56 AT oliverantonyw aroleofthense4kleisinandnse1nse3kitesubunitsintheatpasecycleofsmc56 AT palecekjanj aroleofthense4kleisinandnse1nse3kitesubunitsintheatpasecycleofsmc56 AT vondrovalucie roleofthense4kleisinandnse1nse3kitesubunitsintheatpasecycleofsmc56 AT kolesarpeter roleofthense4kleisinandnse1nse3kitesubunitsintheatpasecycleofsmc56 AT adamusmarek roleofthense4kleisinandnse1nse3kitesubunitsintheatpasecycleofsmc56 AT nociarmatej roleofthense4kleisinandnse1nse3kitesubunitsintheatpasecycleofsmc56 AT oliverantonyw roleofthense4kleisinandnse1nse3kitesubunitsintheatpasecycleofsmc56 AT palecekjanj roleofthense4kleisinandnse1nse3kitesubunitsintheatpasecycleofsmc56 |