دورية أكاديمية
Nse5/6 inhibits the Smc5/6 ATPase and modulates DNA substrate binding.
| العنوان: | Nse5/6 inhibits the Smc5/6 ATPase and modulates DNA substrate binding. |
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| المؤلفون: | Taschner, M., Basquin, J., Steigenberger, B., Schäfer, I.B., Soh, Y.M., Basquin, C., Lorentzen, E., Räschle, M., Scheltema, R.A., Gruber, S. |
| المصدر: | The EMBO journal, vol. 40, no. 15, pp. e107807 |
| سنة النشر: | 2021 |
| المجموعة: | Université de Lausanne (UNIL): Serval - Serveur académique lausannois |
| مصطلحات موضوعية: | Adenosine Triphosphate/metabolism, Cell Cycle Proteins/chemistry, Cell Cycle Proteins/genetics, Cell Cycle Proteins/metabolism, Chromosomal Proteins, Non-Histone/chemistry, Non-Histone/genetics, Non-Histone/metabolism, Cryoelectron Microscopy, Crystallography, X-Ray, DNA, Fungal/metabolism, Hydrolysis, Multiprotein Complexes/chemistry, Multiprotein Complexes/metabolism, Protein Conformation, Saccharomyces cerevisiae/metabolism, Saccharomyces cerevisiae Proteins/chemistry, Saccharomyces cerevisiae Proteins/genetics, Saccharomyces cerevisiae Proteins/metabolism, Smc5/6, chromosome segregation, cohesion, condensin, loop extrusion |
| الوصف: | 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. |
| نوع الوثيقة: | article in journal/newspaper |
| وصف الملف: | application/pdf |
| اللغة: | English |
| تدمد: | 0261-4189 |
| العلاقة: | info:eu-repo/semantics/altIdentifier/pmid/34191293; info:eu-repo/semantics/altIdentifier/eissn/1460-2075; info:eu-repo/semantics/altIdentifier/urn/urn:nbn:ch:serval-BIB_43B3495591E91; https://serval.unil.ch/notice/serval:BIB_43B3495591E9Test; urn:issn:0261-4189; https://serval.unil.ch/resource/serval:BIB_43B3495591E9.P001/REF.pdfTest; http://nbn-resolving.org/urn/resolver.pl?urn=urn:nbn:ch:serval-BIB_43B3495591E91Test |
| DOI: | 10.15252/embj.2021107807 |
| الإتاحة: | https://doi.org/10.15252/embj.2021107807Test https://serval.unil.ch/notice/serval:BIB_43B3495591E9Test https://serval.unil.ch/resource/serval:BIB_43B3495591E9.P001/REF.pdfTest http://nbn-resolving.org/urn/resolver.pl?urn=urn:nbn:ch:serval-BIB_43B3495591E91Test |
| حقوق: | info:eu-repo/semantics/openAccess ; CC BY 4.0 ; https://creativecommons.org/licenses/by/4.0Test/ |
| رقم الانضمام: | edsbas.D15ECCF4 |
| قاعدة البيانات: | BASE |
Full Text Finder | تدمد: | 02614189 |
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| DOI: | 10.15252/embj.2021107807 |