Solution structure and DNA-binding properties of the winged helix domain of the meiotic recombination HOP2 protein

Hem Moktan; Michel F. Guiraldelli; Craig A. Eyster; Weixing Zhao; Chih Ying Lee; Timothy Mather; R. Daniel Camerini-Otero; Patrick Sung; Donghua H. Zhou; Roberto J. Pezza

doi:10.1074/jbc.M114.548180

Solution structure and DNA-binding properties of the winged helix domain of the meiotic recombination HOP2 protein

Hem Moktan, Michel F. Guiraldelli, Craig A. Eyster, Weixing Zhao, Chih Ying Lee, Timothy Mather, R. Daniel Camerini-Otero, Patrick Sung, Donghua H. Zhou, Roberto J. Pezza

Producción científica: Article › revisión exhaustiva

12 Citas (Scopus)

Resumen

Background: HOP2 protein promotes recombination and is required for meiotic chromosome synapsis. Results: The N terminus of HOP2 has a winged head DNA binding structure. Conclusion: The solution structure of the winged head DNA binding domain integrates biochemical and functional aspects of HOP2 recombinational function. Significance: Determining the three-dimensional structure of HOP2 is crucial to understand the mechanism of HOP2 action.

Idioma original	English (US)
Páginas (desde-hasta)	14682-14691
Número de páginas	10
Publicación	Journal of Biological Chemistry
Volumen	289
N.º	21
DOI	https://doi.org/10.1074/jbc.M114.548180
Estado	Published - 2014
Publicado de forma externa	Sí

ASJC Scopus subject areas

Molecular Biology
Biochemistry
Cell Biology

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title = "Solution structure and DNA-binding properties of the winged helix domain of the meiotic recombination HOP2 protein",

abstract = "Background: HOP2 protein promotes recombination and is required for meiotic chromosome synapsis. Results: The N terminus of HOP2 has a winged head DNA binding structure. Conclusion: The solution structure of the winged head DNA binding domain integrates biochemical and functional aspects of HOP2 recombinational function. Significance: Determining the three-dimensional structure of HOP2 is crucial to understand the mechanism of HOP2 action.",

author = "Hem Moktan and Guiraldelli, {Michel F.} and Eyster, {Craig A.} and Weixing Zhao and Lee, {Chih Ying} and Timothy Mather and Camerini-Otero, {R. Daniel} and Patrick Sung and Zhou, {Donghua H.} and Pezza, {Roberto J.}",

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AU - Moktan, Hem

AU - Guiraldelli, Michel F.

AU - Eyster, Craig A.

AU - Zhao, Weixing

AU - Lee, Chih Ying

AU - Mather, Timothy

AU - Camerini-Otero, R. Daniel

AU - Sung, Patrick

AU - Zhou, Donghua H.

AU - Pezza, Roberto J.

PY - 2014

Y1 - 2014

N2 - Background: HOP2 protein promotes recombination and is required for meiotic chromosome synapsis. Results: The N terminus of HOP2 has a winged head DNA binding structure. Conclusion: The solution structure of the winged head DNA binding domain integrates biochemical and functional aspects of HOP2 recombinational function. Significance: Determining the three-dimensional structure of HOP2 is crucial to understand the mechanism of HOP2 action.

AB - Background: HOP2 protein promotes recombination and is required for meiotic chromosome synapsis. Results: The N terminus of HOP2 has a winged head DNA binding structure. Conclusion: The solution structure of the winged head DNA binding domain integrates biochemical and functional aspects of HOP2 recombinational function. Significance: Determining the three-dimensional structure of HOP2 is crucial to understand the mechanism of HOP2 action.

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JO - Journal of Biological Chemistry

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Solution structure and DNA-binding properties of the winged helix domain of the meiotic recombination HOP2 protein

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