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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Hochkoeppler, Alejandro Gawel, Damian Schaaper, Roel M. London, Robert E. Krahn, Juno M. Itsko, Mark Singh, Deepa |
| Description | Author Affiliation: Singh D ( From the Genome Integrity and Structural Biology Laboratory, National Institute of Environmental Health Sciences, National Institutes of Health, Research Triangle Park, North Carolina 27709.); Gawel D ( the Department of Biochemistry and Molecular Biology, Center of Postgraduate Medical Education, 01-813 Warsaw, Poland, and.); Itsko M ( From the Genome Integrity and Structural Biology Laboratory, National Institute of Environmental Health Sciences, National Institutes of Health, Research Triangle Park, North Carolina 27709.); Hochkoeppler A ( the Department of Industrial Chemistry, University of Bologna, 40136 Bologna, Italy.); Krahn JM ( From the Genome Integrity and Structural Biology Laboratory, National Institute of Environmental Health Sciences, National Institutes of Health, Research Triangle Park, North Carolina 27709.); London RE ( From the Genome Integrity and Structural Biology Laboratory, National Institute of Environmental Health Sciences, National Institutes of Health, Research Triangle Park, North Carolina 27709.); Schaaper RM ( From the Genome Integrity and Structural Biology Laboratory, National Institute of Environmental Health Sciences, National Institutes of Health, Research Triangle Park, North Carolina 27709, schaaper@niehs.nih.gov.) |
| Abstract | The Escherichia coli dgt gene encodes a dGTP triphosphohydrolase whose detailed role still remains to be determined. Deletion of dgt creates a mutator phenotype, indicating that the dGTPase has a fidelity role, possibly by affecting the cellular dNTP pool. In the present study, we have investigated the structure of the Dgt protein at 3.1-Å resolution. One of the obtained structures revealed a protein hexamer that contained two molecules of single-stranded DNA. The presence of DNA caused significant conformational changes in the enzyme, including in the catalytic site of the enzyme. Dgt preparations lacking DNA were able to bind single-stranded DNA with high affinity (Kd â ¼ 50 nM). DNA binding positively affected the activity of the enzyme: dGTPase activity displayed sigmoidal (cooperative) behavior without DNA but hyperbolic (Michaelis-Menten) kinetics in its presence, consistent with a specific lowering of the apparent Km for dGTP. A mutant Dgt enzyme was also created containing residue changes in the DNA binding cleft. This mutant enzyme, whereas still active, was incapable of DNA binding and could no longer be stimulated by addition of DNA. We also created an E. coli strain containing the mutant dgt gene on the chromosome replacing the wild-type gene. The mutant also displayed a mutator phenotype. Our results provide insight into the allosteric regulation of the enzyme and support a physiologically important role of DNA binding. |
| ISSN | 00219258 |
| e-ISSN | 1083351X |
| Journal | Journal of Biological Chemistry |
| Issue Number | 16 |
| Volume Number | 290 |
| Language | English |
| Publisher | American Society for Biochemistry and Molecular Biology (United States) |
| Publisher Date | 2015-04-17 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | DNA, Bacterial Chemistry Deoxyguanine Nucleotides Escherichia Coli Proteins Escherichia Coli Enzymology Gene Expression Regulation, Bacterial Phosphoric Monoester Hydrolases Allosteric Regulation Catalytic Domain Chromosomes, Bacterial Metabolism Crystallography, X-Ray DNA-Binding Proteins Genetics Kinetics Models, Molecular Mutation Protein Multimerization Protein Structure, Secondary Recombinant Proteins Research Support, N.I.H., Intramural Research Support, U.S. Gov't, Non-P.H.S. Biochemistry Molecular Biology |
| Content Type | Text |
| Resource Type | Article |
| Subject | Cell Biology Biochemistry Molecular Biology |
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