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  Nse5/6 inhibits the Smc5/6 ATPase and modulates DNA substrate binding

Taschner, M., Basquin, J., Steigenberger, B., Schäfer, I. B., Soh, Y.-M., Basquin, C., et al. (2021). Nse5/6 inhibits the Smc5/6 ATPase and modulates DNA substrate binding. EMBO Journal, e107807. doi:10.15252/embj.2021107807.

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 Creators:
Taschner, Michael1, Author
Basquin, Jerome2, Author              
Steigenberger, Barbara2, Author              
Schäfer, Ingmar B.3, Author              
Soh, Young-Min1, Author
Basquin, Claire3, Author              
Lorentzen, Esben1, Author
Raeschle, Markus1, Author
Scheltema, Richard A.1, Author
Gruber, Stephan1, Author
Affiliations:
1external, ou_persistent22              
2Scientific Service Groups, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565170              
3Conti, Elena / Structural Cell Biology, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565144              

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Free keywords: ELEMENT 5 NSE5; SMC5-SMC6 COMPLEX; SUMO LIGASE; EVOLUTIONARY CONSERVATION; STRUCTURAL BASIS; PROTEIN; REPAIR; CONDENSIN; MECHANISM; SUBUNITBiochemistry & Molecular Biology; Cell Biology; chromosome segregation; cohesion; condensin; loop extrusion; Smc5; 6;
 Abstract: Eukaryotic cells employ three SMC (structural maintenance of chromosomes) complexes to control DNA folding and topology. The Smc5/6 complex plays roles in DNA repair and in preventing the accumulation of deleterious DNA junctions. To elucidate how specific features of Smc5/6 govern these functions, we reconstituted the yeast holo-complex. We found that the Nse5/6 sub-complex strongly inhibited the Smc5/6 ATPase by preventing productive ATP binding. This inhibition was relieved by plasmid DNA binding but not by short linear DNA, while opposing effects were observed without Nse5/6. We uncovered two binding sites for Nse5/6 on Smc5/6, based on an Nse5/6 crystal structure and cross-linking mass spectrometry data. One binding site is located at the Smc5/6 arms and one at the heads, the latter likely exerting inhibitory effects on ATP hydrolysis. Cysteine cross-linking demonstrated that the interaction with Nse5/6 anchored the ATPase domains in a non-productive state, which was destabilized by ATP and DNA. Under similar conditions, the Nse4/3/1 module detached from the ATPase. Altogether, we show how DNA substrate selection is modulated by direct inhibition of the Smc5/6 ATPase by Nse5/6.

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Language(s): eng - English
 Dates: 2021
 Publication Status: Published online
 Pages: 23
 Publishing info: -
 Table of Contents: -
 Rev. Type: -
 Identifiers: ISI: 000668244800001
DOI: 10.15252/embj.2021107807
 Degree: -

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Title: EMBO Journal
  Other : EMBO J.
Source Genre: Journal
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Publ. Info: Nature Publishing Group
Pages: - Volume / Issue: - Sequence Number: e107807 Start / End Page: - Identifier: ISSN: 0261-4189
CoNE: https://pure.mpg.de/cone/journals/resource/954925497061