دورية أكاديمية
أعرض في EDS

Using energy to go downhill-a genoprotective role for ATPase activity in DNA topoisomerase II.

التفاصيل البيبلوغرافية
العنوان: Using energy to go downhill-a genoprotective role for ATPase activity in DNA topoisomerase II.
المؤلفون: Bandak AF; Johns Hopkins University School of Medicine, Department of Biophysics and Biophysical Chemistry, Baltimore, MD 21205, USA., Blower TR; Johns Hopkins University School of Medicine, Department of Biophysics and Biophysical Chemistry, Baltimore, MD 21205, USA., Nitiss KC; Pharmaceutical Sciences Department, University of Illinois College of Pharmacy, 1601 Parkview Avenue, Rockford, IL 61107, USA.; Biomedical Sciences Department, University of Illinois College of Medicine, 1601 Parkview Avenue, Rockford, IL 61107, USA., Shah V; Pharmaceutical Sciences Department, University of Illinois College of Pharmacy, 1601 Parkview Avenue, Rockford, IL 61107, USA.; Biomedical Sciences Department, University of Illinois College of Medicine, 1601 Parkview Avenue, Rockford, IL 61107, USA., Nitiss JL; Pharmaceutical Sciences Department, University of Illinois College of Pharmacy, 1601 Parkview Avenue, Rockford, IL 61107, USA., Berger JM; Johns Hopkins University School of Medicine, Department of Biophysics and Biophysical Chemistry, Baltimore, MD 21205, USA.
المصدر: Nucleic acids research [Nucleic Acids Res] 2024 Feb 09; Vol. 52 (3), pp. 1313-1324.
نوع المنشور: Journal Article
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: DNA*/genetics , DNA Topoisomerases, Type II*/genetics, Humans ; Adenosine Triphosphatases/genetics ; Adenosine Triphosphate ; Etoposide/pharmacology ; DNA Damage
مستخلص: Type II topoisomerases effect topological changes in DNA by cutting a single duplex, passing a second duplex through the break, and resealing the broken strand in an ATP-coupled reaction cycle. Curiously, most type II topoisomerases (topos II, IV and VI) catalyze DNA transformations that are energetically favorable, such as the removal of superhelical strain; why ATP is required for such reactions is unknown. Here, using human topoisomerase IIβ (hTOP2β) as a model, we show that the ATPase domains of the enzyme are not required for DNA strand passage, but that their loss elevates the enzyme's propensity for DNA damage. The unstructured C-terminal domains (CTDs) of hTOP2β strongly potentiate strand passage activity in ATPase-less enzymes, as do cleavage-prone mutations that confer hypersensitivity to the chemotherapeutic agent etoposide. The presence of either the CTD or the mutations lead ATPase-less enzymes to promote even greater levels of DNA cleavage in vitro, as well as in vivo. By contrast, aberrant cleavage phenotypes of these topo II variants is significantly repressed when the ATPase domains are present. Our findings are consistent with the proposal that type II topoisomerases acquired ATPase function to maintain high levels of catalytic activity while minimizing inappropriate DNA damage.
(© The Author(s) 2023. Published by Oxford University Press on behalf of Nucleic Acids Research.)
التعليقات: Update of: bioRxiv. 2023 Jun 27;:. (PMID: 37425896)
Erratum in: Nucleic Acids Res. 2023 Dec 28;:. (PMID: 38153185)
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معلومات مُعتمدة: R01 CA077373 United States CA NCI NIH HHS; R03 CA259884 United States CA NCI NIH HHS; R03 NS116666 United States NS NINDS NIH HHS; T32-GM008403-28 United States NH NIH HHS
المشرفين على المادة: EC 3.6.1.- (Adenosine Triphosphatases)
8L70Q75FXE (Adenosine Triphosphate)
9007-49-2 (DNA)
EC 5.99.1.3 (DNA Topoisomerases, Type II)
6PLQ3CP4P3 (Etoposide)
تواريخ الأحداث: Date Created: 20231201 Date Completed: 20240214 Latest Revision: 20240219
رمز التحديث: 20240219
مُعرف محوري في PubMed: PMC10853770
DOI: 10.1093/nar/gkad1157
PMID: 38038260
قاعدة البيانات: MEDLINE
الوصف
تدمد:1362-4962
DOI:10.1093/nar/gkad1157