A human topoisomerase IIα heterodimer with only one ATP binding site can go through successive catalytic cycles

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A human topoisomerase IIα heterodimer with only one ATP binding site can go through successive catalytic cycles. / Skouboe, Camilla; Bjergbaek, Lotte; Oestergaard, Vibe H.; Larsen, Morten K.; Knudsen, Birgitta R.; Andersen, Anni H.

I: Journal of Biological Chemistry, Bind 278, Nr. 8, 21.02.2003, s. 5768-5774.

Publikation: Bidrag til tidsskriftTidsskriftartikelfagfællebedømt

Harvard

Skouboe, C, Bjergbaek, L, Oestergaard, VH, Larsen, MK, Knudsen, BR & Andersen, AH 2003, 'A human topoisomerase IIα heterodimer with only one ATP binding site can go through successive catalytic cycles', Journal of Biological Chemistry, bind 278, nr. 8, s. 5768-5774. https://doi.org/10.1074/jbc.M210332200

APA

Skouboe, C., Bjergbaek, L., Oestergaard, V. H., Larsen, M. K., Knudsen, B. R., & Andersen, A. H. (2003). A human topoisomerase IIα heterodimer with only one ATP binding site can go through successive catalytic cycles. Journal of Biological Chemistry, 278(8), 5768-5774. https://doi.org/10.1074/jbc.M210332200

Vancouver

Skouboe C, Bjergbaek L, Oestergaard VH, Larsen MK, Knudsen BR, Andersen AH. A human topoisomerase IIα heterodimer with only one ATP binding site can go through successive catalytic cycles. Journal of Biological Chemistry. 2003 feb. 21;278(8):5768-5774. https://doi.org/10.1074/jbc.M210332200

Author

Skouboe, Camilla ; Bjergbaek, Lotte ; Oestergaard, Vibe H. ; Larsen, Morten K. ; Knudsen, Birgitta R. ; Andersen, Anni H. / A human topoisomerase IIα heterodimer with only one ATP binding site can go through successive catalytic cycles. I: Journal of Biological Chemistry. 2003 ; Bind 278, Nr. 8. s. 5768-5774.

Bibtex

@article{ad224ab7d6344bb6b23edf6327cc9469,
title = "A human topoisomerase IIα heterodimer with only one ATP binding site can go through successive catalytic cycles",
abstract = "Eukaryotic DNA topoisomerase II is a dimeric nuclear enzyme essential for DNA metabolism and chromosome dynamics. It changes the topology of DNA by coupling binding and hydrolysis of two ATP molecules to the transport of one DNA duplex through a temporary break introduced in another. During this process the structurally and functionally complex enzyme passes through a cascade of conformational changes, which requires intra- and intersubunit communication. To study the importance of ATP binding and hydrolysis in relation to DNA strand transfer, we have purified and characterized a human topoisomerase IIα heterodimer with only one ATP binding site. The heterodimer was able to relax supercoiled DNA, although less efficiently than the wild type enzyme. It furthermore possessed a functional N-terminal clamp and was sensitive to ICRF-187. This demonstrates that human topoisomerase IIα can pass through all the conformations required for DNA strand passage and enzyme resetting with binding and hydrolysis of only one ATP. However, the heterodimer lacked the normal stimulatory effect of DNA on ATP binding and hydrolysis as well as the stimulatory effect of ATP on DNA cleavage. The results can be explained in a model, where efficient catalysis requires an extensive communication between the second ATP and the DNA segment to be cleaved.",
author = "Camilla Skouboe and Lotte Bjergbaek and Oestergaard, {Vibe H.} and Larsen, {Morten K.} and Knudsen, {Birgitta R.} and Andersen, {Anni H.}",
year = "2003",
month = feb,
day = "21",
doi = "10.1074/jbc.M210332200",
language = "English",
volume = "278",
pages = "5768--5774",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology, Inc.",
number = "8",

}

RIS

TY - JOUR

T1 - A human topoisomerase IIα heterodimer with only one ATP binding site can go through successive catalytic cycles

AU - Skouboe, Camilla

AU - Bjergbaek, Lotte

AU - Oestergaard, Vibe H.

AU - Larsen, Morten K.

AU - Knudsen, Birgitta R.

AU - Andersen, Anni H.

PY - 2003/2/21

Y1 - 2003/2/21

N2 - Eukaryotic DNA topoisomerase II is a dimeric nuclear enzyme essential for DNA metabolism and chromosome dynamics. It changes the topology of DNA by coupling binding and hydrolysis of two ATP molecules to the transport of one DNA duplex through a temporary break introduced in another. During this process the structurally and functionally complex enzyme passes through a cascade of conformational changes, which requires intra- and intersubunit communication. To study the importance of ATP binding and hydrolysis in relation to DNA strand transfer, we have purified and characterized a human topoisomerase IIα heterodimer with only one ATP binding site. The heterodimer was able to relax supercoiled DNA, although less efficiently than the wild type enzyme. It furthermore possessed a functional N-terminal clamp and was sensitive to ICRF-187. This demonstrates that human topoisomerase IIα can pass through all the conformations required for DNA strand passage and enzyme resetting with binding and hydrolysis of only one ATP. However, the heterodimer lacked the normal stimulatory effect of DNA on ATP binding and hydrolysis as well as the stimulatory effect of ATP on DNA cleavage. The results can be explained in a model, where efficient catalysis requires an extensive communication between the second ATP and the DNA segment to be cleaved.

AB - Eukaryotic DNA topoisomerase II is a dimeric nuclear enzyme essential for DNA metabolism and chromosome dynamics. It changes the topology of DNA by coupling binding and hydrolysis of two ATP molecules to the transport of one DNA duplex through a temporary break introduced in another. During this process the structurally and functionally complex enzyme passes through a cascade of conformational changes, which requires intra- and intersubunit communication. To study the importance of ATP binding and hydrolysis in relation to DNA strand transfer, we have purified and characterized a human topoisomerase IIα heterodimer with only one ATP binding site. The heterodimer was able to relax supercoiled DNA, although less efficiently than the wild type enzyme. It furthermore possessed a functional N-terminal clamp and was sensitive to ICRF-187. This demonstrates that human topoisomerase IIα can pass through all the conformations required for DNA strand passage and enzyme resetting with binding and hydrolysis of only one ATP. However, the heterodimer lacked the normal stimulatory effect of DNA on ATP binding and hydrolysis as well as the stimulatory effect of ATP on DNA cleavage. The results can be explained in a model, where efficient catalysis requires an extensive communication between the second ATP and the DNA segment to be cleaved.

UR - http://www.scopus.com/inward/record.url?scp=0037458744&partnerID=8YFLogxK

U2 - 10.1074/jbc.M210332200

DO - 10.1074/jbc.M210332200

M3 - Journal article

C2 - 12480934

AN - SCOPUS:0037458744

VL - 278

SP - 5768

EP - 5774

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 8

ER -

ID: 238744593