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

Research output: Contribution to journal › Article › peer-review

12 Scopus citations

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.

Original language	English (US)
Pages (from-to)	14682-14691
Number of pages	10
Journal	Journal of Biological Chemistry
Volume	289
Issue number	21
DOIs	https://doi.org/10.1074/jbc.M114.548180
State	Published - 2014
Externally published	Yes

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.}",

year = "2014",

doi = "10.1074/jbc.M114.548180",

language = "English (US)",

volume = "289",

pages = "14682--14691",

journal = "Journal of Biological Chemistry",

issn = "0021-9258",

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T1 - Solution structure and DNA-binding properties of the winged helix domain of the meiotic recombination HOP2 protein

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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DO - 10.1074/jbc.M114.548180

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AN - SCOPUS:84901451522

SN - 0021-9258

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SP - 14682

EP - 14691

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

IS - 21

ER -

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

Abstract

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