The characterization of stem-loop RNA binding protein-ribosomal protein P0
| Autor: | DENNIS HONG, 洪瑞陽 |
|---|---|
| Rok vydání: | 2000 |
| Druh dokumentu: | 學位論文 ; thesis |
| Popis: | 88 We obtained a mutant m4(-) derived from E.coli strain XL1-Blue MRF'' with a mutation in priB gene. The mutated priB gene contains a point mutation and leads to a single amino acid substitution from Phe to Val at position 77. However, no direct evidence has been described for the role of PriB in replication in vivo. The mutant strain m4(-) significantly reduces the copy number of the Δrop ColE1-type plasmid. With the feature of reducing plasmid copy number, we suppose PriB is a conserved protein in evolution. Using this mutant strain, we tried find out the complementary protein by screening HeLa cell cDNA library. After selection, we obtained five candidates: P0 protein, heat shock protein 90S, rabaptin, glutamate transporter, synaptogyrin 2 (SYNGR2). P0 protein is a ribosomal protein with apurinic /apyrimidinic endonuclease activity when overexpressed in Drosophila. The DNA binding domain is the functional domain of P0 protein to complement the defect of PriB. Previous studies have shown that P0 is a multifunction protein, but the detail bio-pathway is still unclear. By two-hybrid assay, we obtained two candidates: P1 and High density lipoprotein binding protein (vigilin). In this thesis, we have detailed description about the pathway of protein- protein interaction. Furthermore, more and more studies showed that P0 is overexpressed in several cancer. We also find that P0 is overexpressed in breast cancer. Further biochemical studies will be focused on… |
| Databáze: | Networked Digital Library of Theses & Dissertations |
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