دورية أكاديمية
أعرض في EDS

Condensin extrudes DNA loops in steps up to hundreds of base pairs that are generated by ATP binding events.

التفاصيل البيبلوغرافية
العنوان: Condensin extrudes DNA loops in steps up to hundreds of base pairs that are generated by ATP binding events.
المؤلفون: Ryu JK; Department of Bionanoscience, Kavli Institute of Nanoscience Delft, Delft University of Technology, 2629 HZ Delft, The Netherlands., Rah SH; Department of Bionanoscience, Kavli Institute of Nanoscience Delft, Delft University of Technology, 2629 HZ Delft, The Netherlands., Janissen R; Department of Bionanoscience, Kavli Institute of Nanoscience Delft, Delft University of Technology, 2629 HZ Delft, The Netherlands., Kerssemakers JWJ; Department of Bionanoscience, Kavli Institute of Nanoscience Delft, Delft University of Technology, 2629 HZ Delft, The Netherlands., Bonato A; University of Edinburgh, SUPA, School of Physics and Astronomy, EH9 3FD, Edinburgh, UK., Michieletto D; University of Edinburgh, SUPA, School of Physics and Astronomy, EH9 3FD, Edinburgh, UK.; MRC Human Genetics Unit, Institute of Genetics and Cancer, University of Edinburgh, Edinburgh EH4 2XU, UK., Dekker C; Department of Bionanoscience, Kavli Institute of Nanoscience Delft, Delft University of Technology, 2629 HZ Delft, The Netherlands.
المصدر: Nucleic acids research [Nucleic Acids Res] 2022 Jan 25; Vol. 50 (2), pp. 820-832.
نوع المنشور: Journal Article; Research Support, Non-U.S. Gov't
اللغة: English
بيانات الدورية: Publisher: Oxford University Press Country of Publication: England NLM ID: 0411011 Publication Model: Print Cited Medium: Internet ISSN: 1362-4962 (Electronic) Linking ISSN: 03051048 NLM ISO Abbreviation: Nucleic Acids Res Subsets: MEDLINE
أسماء مطبوعة: Publication: 1992- : Oxford : Oxford University Press
Original Publication: London, Information Retrieval ltd.
مواضيع طبية MeSH: Adenosine Triphosphatases/*metabolism , Chromatin/*metabolism , DNA, Fungal/*metabolism , DNA-Binding Proteins/*metabolism , Multiprotein Complexes/*metabolism , Saccharomyces cerevisiae/*genetics , Saccharomyces cerevisiae Proteins/*metabolism, Nucleic Acid Conformation ; Protein Binding
مستخلص: The condensin SMC protein complex organizes chromosomal structure by extruding loops of DNA. Its ATP-dependent motor mechanism remains unclear but likely involves steps associated with large conformational changes within the ∼50 nm protein complex. Here, using high-resolution magnetic tweezers, we resolve single steps in the loop extrusion process by individual yeast condensins. The measured median step sizes range between 20-40 nm at forces of 1.0-0.2 pN, respectively, comparable with the holocomplex size. These large steps show that, strikingly, condensin typically reels in DNA in very sizeable amounts with ∼200 bp on average per single extrusion step at low force, and occasionally even much larger, exceeding 500 bp per step. Using Molecular Dynamics simulations, we demonstrate that this is due to the structural flexibility of the DNA polymer at these low forces. Using ATP-binding-impaired and ATP-hydrolysis-deficient mutants, we find that ATP binding is the primary step-generating stage underlying DNA loop extrusion. We discuss our findings in terms of a scrunching model where a stepwise DNA loop extrusion is generated by an ATP-binding-induced engagement of the hinge and the globular domain of the SMC complex.
(© The Author(s) 2021. Published by Oxford University Press on behalf of Nucleic Acids Research.)
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المشرفين على المادة: 0 (Chromatin)
0 (DNA, Fungal)
0 (DNA-Binding Proteins)
0 (Multiprotein Complexes)
0 (Saccharomyces cerevisiae Proteins)
0 (condensin complexes)
EC 3.6.1.- (Adenosine Triphosphatases)
تواريخ الأحداث: Date Created: 20211224 Date Completed: 20220221 Latest Revision: 20220221
رمز التحديث: 20240628
مُعرف محوري في PubMed: PMC8789078
DOI: 10.1093/nar/gkab1268
PMID: 34951453
قاعدة البيانات: MEDLINE
الوصف
تدمد:1362-4962
DOI:10.1093/nar/gkab1268