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Tytuł:
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Remodeling Chromatin Induces Z-DNA Conformation Detected through Fourier Transform Infrared Spectroscopy.
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Autorzy:
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Li Y; Henan Key Laboratory of Ion-beam Bioengineering, School of Physics and Microelectronics, Zhengzhou University, Zhengzhou 450001, China.
Huang Q; CAS Key Laboratory of Ion-beam Bioengineering, Hefei Institutes of Physical Science, Institute of Intelligent Machines, Chinese Academy of Sciences (CAS), Hefei 230031, China.
Yao G; CAS Key Laboratory of Ion-beam Bioengineering, Hefei Institutes of Physical Science, Institute of Intelligent Machines, Chinese Academy of Sciences (CAS), Hefei 230031, China.
Wang X; Department of Pediatric Hematology and Oncology, Zhengzhou University First Affiliated Hospital, Zhengzhou 450000 China.
Zhang F; Henan Key Laboratory of Ion-beam Bioengineering, School of Physics and Microelectronics, Zhengzhou University, Zhengzhou 450001, China.
Wang T; The College of Nursing and Health, Zhengzhou University, Zhengzhou, China 450001.
Shao C; CAS Key Laboratory of Ion-beam Bioengineering, Hefei Institutes of Physical Science, Institute of Intelligent Machines, Chinese Academy of Sciences (CAS), Hefei 230031, China.
Zheng X; CAS Key Laboratory of Ion-beam Bioengineering, Hefei Institutes of Physical Science, Institute of Intelligent Machines, Chinese Academy of Sciences (CAS), Hefei 230031, China.
Jing X; Henan Key Laboratory of Ion-beam Bioengineering, School of Physics and Microelectronics, Zhengzhou University, Zhengzhou 450001, China.
Zhou H; The College of Nursing and Health, Zhengzhou University, Zhengzhou, China 450001.
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Źródło:
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Analytical chemistry [Anal Chem] 2020 Nov 03; Vol. 92 (21), pp. 14452-14458. Date of Electronic Publication: 2020 Oct 21.
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Typ publikacji:
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Journal Article; Research Support, Non-U.S. Gov't
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Język:
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English
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Imprint Name(s):
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Original Publication: Washington, American Chemical Society.
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MeSH Terms:
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Chromatin Assembly and Disassembly*
Nucleic Acid Conformation*
Spectroscopy, Fourier Transform Infrared*
DNA, Z-Form/*chemistry
Adenosine Triphosphate/metabolism ; Cell Line, Tumor ; DNA Helicases/deficiency ; DNA Helicases/genetics ; DNA, Z-Form/metabolism ; Gene Knockdown Techniques ; Humans ; Nuclear Proteins/deficiency ; Nuclear Proteins/genetics ; Transcription Factors/deficiency ; Transcription Factors/genetics
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Substance Nomenclature:
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0 (DNA, Z-Form)
0 (Nuclear Proteins)
0 (Transcription Factors)
8L70Q75FXE (Adenosine Triphosphate)
EC 3.6.1.- (SMARCA4 protein, human)
EC 3.6.4.- (DNA Helicases)
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Entry Date(s):
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Date Created: 20201021 Date Completed: 20210222 Latest Revision: 20210222
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Update Code:
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20240105
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DOI:
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10.1021/acs.analchem.0c02432
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PMID:
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33085464
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The SWI/SNF complex is a highly conserved chromatin remodeling complex and can hydrolyze ATP by its catalytic subunit BRG1 or BRM to reconstruct the chromatin. To investigate whether this ATP-dependent chromatin remodeling could affect the DNA conformation, we therefore regulated (knocked down or overexpressed) BRG1/BRM in the cells and applied Fourier transform infrared (FTIR) spectroscopy to probe DNA conformational changes. As a result, we found that BRG1/BRM was indeed associated with the DNA conformational changes, in which knockdown of BRG1/BRM reduced Z-DNA conformation, while overexpression of BRG1/BRM enhanced Z-DNA conformation. This Z-DNA conformational transformation was also verified using the Z-DNA-binding proteins. Therefore, this work has provided a direct analytical tool to probe Z-DNA transformation upon ATP-dependent chromatin remodeling.