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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Su, Guan-chin Chi, Peter Chang, Hao-yen Liao, Chia-yu Lin, Sheng-wei Wang, Hong-wei |
| Description | Author Affiliation: Chang HY ( From the Institute of Biochemical Sciences, National Taiwan University, Number 1, Section 4, Roosevelt Road, Taipei 10617 Taiwan.); Liao CY ( From the Institute of Biochemical Sciences, National Taiwan University, Number 1, Section 4, Roosevelt Road, Taipei 10617 Taiwan.); Su GC ( From the Institute of Biochemical Sciences, National Taiwan University, Number 1, Section 4, Roosevelt Road, Taipei 10617 Taiwan.); Lin SW ( the Institute of Biological Chemistry, Academia Sinica, 128 Academia Road, Section 2, Nankang, Taipei 11529, Taiwan, and.); Wang HW ( the Ministry of Education Key Laboratory of Protein Science, Tsinghua-Peking Joint Center for Life Sciences, Center for Structural Biology, School of Life Sciences, Tsinghua University, Beijing 100084, China.); Chi P ( From the Institute of Biochemical Sciences, National Taiwan University, Number 1, Section 4, Roosevelt Road, Taipei 10617 Taiwan, the Institute of Biological Chemistry, Academia Sinica, 128 Academia Road, Section 2, Nankang, Taipei 11529, Taiwan, and peterhchi@ntu.edu.tw.) |
| Abstract | DMC1 and RAD51 are conserved recombinases that catalyze homologous recombination. DMC1 and RAD51 share similar properties in DNA binding, DNA-stimulated ATP hydrolysis, and catalysis of homologous DNA strand exchange. A large body of evidence indicates that attenuation of ATP hydrolysis leads to stabilization of the RAD51-ssDNA presynaptic filament and enhancement of DNA strand exchange. However, the functional relationship of ATPase activity, presynaptic filament stability, and DMC1-mediated homologous DNA strand exchange has remained largely unexplored. To address this important question, we have constructed several mutant variants of human DMC1 and characterized them biochemically to gain mechanistic insights. Two mutations, K132R and D223N, that change key residues in the Walker A and B nucleotide-binding motifs ablate ATP binding and render DMC1 inactive. On the other hand, the nucleotide-binding cap D317K mutant binds ATP normally but shows significantly attenuated ATPase activity and, accordingly, forms a highly stable presynaptic filament. Surprisingly, unlike RAD51, presynaptic filament stabilization achieved via ATP hydrolysis attenuation does not lead to any enhancement of DMC1-catalyzed homologous DNA pairing and strand exchange. This conclusion is further supported by examining wild-type DMC1 with non-hydrolyzable ATP analogues. Thus, our results reveal an important mechanistic difference between RAD51 and DMC1. |
| ISSN | 00219258 |
| e-ISSN | 1083351X |
| Journal | Journal of Biological Chemistry |
| Issue Number | 32 |
| Volume Number | 290 |
| Language | English |
| Publisher | American Society for Biochemistry and Molecular Biology (United States) |
| Publisher Date | 2015-08-07 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Cell Cycle Proteins Metabolism Chromosome Pairing DNA, Single-Stranded DNA-Binding Proteins Homologous Recombination Rad51 Recombinase Adenosine Monophosphate Chemistry Adenosine Triphosphate Genetics Escherichia Coli Escherichia Coli Proteins Exodeoxyribonucleases Gene Expression Hydrolysis Molecular Sequence Data Mutation Nucleic Acid Conformation Nucleotide Motifs Protein Binding Recombinant Proteins Research Support, Non-U.S. Gov't Biochemistry Molecular Biology |
| Content Type | Text |
| Resource Type | Article |
| Subject | Cell Biology Biochemistry Molecular Biology |
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