| Content Provider |
World Health Organization (WHO)-Global Index Medicus |
| Author |
Eyster, Craig A. Camerini-otero, R. Daniel Zhou, Donghua H. Mather, Timothy Moktan, Hem Sung, Patrick Pezza, Roberto J. Guiraldelli, Michel F. Lee, Chih-ying Zhao, Weixing |
| Description |
Author Affiliation: Moktan H ( From the Department of Physics, Oklahoma State University, Stillwater, Oklahoma 74078.); Guiraldelli MF ( the Cell Cycle and Cancer Biology Program, Oklahoma Medical Research Foundation, Oklahoma City, Oklahoma 73104.); Eyster CA ( the Cell Cycle and Cancer Biology Program, Oklahoma Medical Research Foundation, Oklahoma City, Oklahoma 73104.); Zhao W ( the Department of Molecular Biophysics and Biochemistry, Yale University School of Medicine, New Haven, Connecticut 06520.); Lee CY ( the Cell Cycle and Cancer Biology Program, Oklahoma Medical Research Foundation, Oklahoma City, Oklahoma 73104.); Mather T ( the Cardiovascular Biology Program, Oklahoma Medical Research Foundation, Oklahoma City, Oklahoma 73104, the Department of Biochemistry and Molecular Biology, Oklahoma University Health Sciences Center, Oklahoma City, Oklahoma 73104.); Camerini-Otero RD ( the Genetics and Biochemistry Branch, NIDDK, National Institutes of Health, Bethesda, Maryland 20892, and.); Sung P ( the Department of Molecular Biophysics and Biochemistry, Yale University School of Medicine, New Haven, Connecticut 06520.); Zhou DH ( From the Department of Physics, Oklahoma State University, Stillwater, Oklahoma 74078.); Pezza RJ ( the Cell Cycle and Cancer Biology Program, Oklahoma Medical Research Foundation, Oklahoma City, Oklahoma 73104, the Department of Cell Biology, Oklahoma University Health Science Center, Oklahoma City, Oklahoma 73126 Roberto-Pezza@omrf.org.) |
| Abstract |
The HOP2 protein is required for efficient double-strand break repair which ensures the proper synapsis of homologous chromosomes and normal meiotic progression. We previously showed that in vitro HOP2 shows two distinctive activities: when it is incorporated into a HOP2-MND1 heterodimer, it stimulates DMC1 and RAD51 recombination activities, and the purified HOP2 alone is proficient in promoting strand invasion. The structural and biochemical basis of HOP2 action in recombination are poorly understood; therefore, they are the focus of this work. Herein, we present the solution structure of the amino-terminal portion of mouse HOP2, which contains a typical winged helix DNA-binding domain. Together with NMR spectral changes in the presence of double-stranded DNA, protein docking on DNA, and mutation analysis to identify the amino acids involved in DNA coordination, our results on the three-dimensional structure of HOP2 provide key information on the fundamental structural and biochemical requirements directing the interaction of HOP2 with DNA. These results, in combination with mutational experiments showing the role of a coiled-coil structural feature involved in HOP2 self-association, allow us to explain important aspects of the function of HOP2 in recombination. |
| ISSN |
00219258 |
| e-ISSN |
1083351X |
| Journal |
Journal of Biological Chemistry |
| Issue Number |
21 |
| Volume Number |
289 |
| Language |
English |
| Publisher |
American Society for Biochemistry and Molecular Biology (United States) |
| Publisher Date |
2014-05-23 |
| Publisher Place |
United States |
| Access Restriction |
Open |
| Subject Keyword |
Cell Cycle Proteins Chemistry DNA-Binding Proteins DNA Protein Structure, Secondary Protein Structure, Tertiary Amino Acid Sequence Amino Acids Genetics Metabolism Animals Binding Sites Magnetic Resonance Spectroscopy Mice Models, Molecular Molecular Sequence Data Mutation Nucleic Acid Conformation Protein Binding Sequence Homology, Amino Acid Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't Biochemistry Molecular Biology |
| Content Type |
Text |
| Resource Type |
Article |
| Subject |
Cell Biology Biochemistry Molecular Biology |
