Aarhus University Seal / Aarhus Universitets segl

Hairpin structures formed by alpha satellite DNA of human centromeres are cleaved by human topoisomerase II alpha

Publikation: Bidrag til tidsskrift/Konferencebidrag i tidsskrift /Bidrag til avisTidsskriftartikelForskningpeer review

Standard

Hairpin structures formed by alpha satellite DNA of human centromeres are cleaved by human topoisomerase II alpha. / Jonstrup, Anette Thyssen; Thomsen, Tina; Wang, Yong; Knudsen, Birgitta R; Koch, Jørn; Andersen, Anni H.

I: Nucleic Acids Research, Bind 36, Nr. 19, 2008, s. 6165-74.

Publikation: Bidrag til tidsskrift/Konferencebidrag i tidsskrift /Bidrag til avisTidsskriftartikelForskningpeer review

Harvard

APA

CBE

MLA

Vancouver

Author

Jonstrup, Anette Thyssen ; Thomsen, Tina ; Wang, Yong ; Knudsen, Birgitta R ; Koch, Jørn ; Andersen, Anni H. / Hairpin structures formed by alpha satellite DNA of human centromeres are cleaved by human topoisomerase II alpha. I: Nucleic Acids Research. 2008 ; Bind 36, Nr. 19. s. 6165-74.

Bibtex

@article{3b00ea90dcb511dd9b3b000ea68e967b,
title = "Hairpin structures formed by alpha satellite DNA of human centromeres are cleaved by human topoisomerase II alpha",
abstract = "Although centromere function has been conserved through evolution, apparently no interspecies consensus DNA sequence exists. Instead, centromere DNA may be interconnected through the formation of certain DNA structures creating topological binding sites for centromeric proteins. DNA topoisomerase II is a protein, which is located at centromeres, and enzymatic topoisomerase II activity correlates with centromere activity in human cells. It is therefore possible that topoisomerase II recognizes and interacts with the alpha satellite DNA of human centromeres through an interaction with potential DNA structures formed solely at active centromeres. In the present study, human topoisomerase IIalpha-mediated cleavage at centromeric DNA sequences was examined in vitro. The investigation has revealed that the enzyme recognizes and cleaves a specific hairpin structure formed by alpha satellite DNA. The topoisomerase introduces a single-stranded break at the hairpin loop in a reaction, where DNA ligation is partly uncoupled from the cleavage reaction. A mutational analysis has revealed, which features of the hairpin are required for topoisomerease IIalpha-mediated cleavage. Based on this a model is discussed, where topoisomerase II interacts with two hairpins as a mediator of centromere cohesion.",
keywords = "Antigens, Neoplasm, Base Sequence, Centromere, DNA Topoisomerases, Type II, Eukaryotic, DNA, Satellite, DNA-Binding Proteins, Enzyme Inhibitors, Humans, Models, Biological, Molecular Sequence Data, Nucleic Acid Conformation, Teniposide",
author = "Jonstrup, {Anette Thyssen} and Tina Thomsen and Yong Wang and Knudsen, {Birgitta R} and J{\o}rn Koch and Andersen, {Anni H}",
year = "2008",
doi = "10.1093/nar/gkn640",
language = "English",
volume = "36",
pages = "6165--74",
journal = "Nucleic Acids Research",
issn = "0305-1048",
publisher = "Oxford University Press",
number = "19",

}

RIS

TY - JOUR

T1 - Hairpin structures formed by alpha satellite DNA of human centromeres are cleaved by human topoisomerase II alpha

AU - Jonstrup, Anette Thyssen

AU - Thomsen, Tina

AU - Wang, Yong

AU - Knudsen, Birgitta R

AU - Koch, Jørn

AU - Andersen, Anni H

PY - 2008

Y1 - 2008

N2 - Although centromere function has been conserved through evolution, apparently no interspecies consensus DNA sequence exists. Instead, centromere DNA may be interconnected through the formation of certain DNA structures creating topological binding sites for centromeric proteins. DNA topoisomerase II is a protein, which is located at centromeres, and enzymatic topoisomerase II activity correlates with centromere activity in human cells. It is therefore possible that topoisomerase II recognizes and interacts with the alpha satellite DNA of human centromeres through an interaction with potential DNA structures formed solely at active centromeres. In the present study, human topoisomerase IIalpha-mediated cleavage at centromeric DNA sequences was examined in vitro. The investigation has revealed that the enzyme recognizes and cleaves a specific hairpin structure formed by alpha satellite DNA. The topoisomerase introduces a single-stranded break at the hairpin loop in a reaction, where DNA ligation is partly uncoupled from the cleavage reaction. A mutational analysis has revealed, which features of the hairpin are required for topoisomerease IIalpha-mediated cleavage. Based on this a model is discussed, where topoisomerase II interacts with two hairpins as a mediator of centromere cohesion.

AB - Although centromere function has been conserved through evolution, apparently no interspecies consensus DNA sequence exists. Instead, centromere DNA may be interconnected through the formation of certain DNA structures creating topological binding sites for centromeric proteins. DNA topoisomerase II is a protein, which is located at centromeres, and enzymatic topoisomerase II activity correlates with centromere activity in human cells. It is therefore possible that topoisomerase II recognizes and interacts with the alpha satellite DNA of human centromeres through an interaction with potential DNA structures formed solely at active centromeres. In the present study, human topoisomerase IIalpha-mediated cleavage at centromeric DNA sequences was examined in vitro. The investigation has revealed that the enzyme recognizes and cleaves a specific hairpin structure formed by alpha satellite DNA. The topoisomerase introduces a single-stranded break at the hairpin loop in a reaction, where DNA ligation is partly uncoupled from the cleavage reaction. A mutational analysis has revealed, which features of the hairpin are required for topoisomerease IIalpha-mediated cleavage. Based on this a model is discussed, where topoisomerase II interacts with two hairpins as a mediator of centromere cohesion.

KW - Antigens, Neoplasm

KW - Base Sequence

KW - Centromere

KW - DNA Topoisomerases, Type II, Eukaryotic

KW - DNA, Satellite

KW - DNA-Binding Proteins

KW - Enzyme Inhibitors

KW - Humans

KW - Models, Biological

KW - Molecular Sequence Data

KW - Nucleic Acid Conformation

KW - Teniposide

U2 - 10.1093/nar/gkn640

DO - 10.1093/nar/gkn640

M3 - Journal article

C2 - 18824478

VL - 36

SP - 6165

EP - 6174

JO - Nucleic Acids Research

JF - Nucleic Acids Research

SN - 0305-1048

IS - 19

ER -