Zebrafish thymidylate synthase binds to its own mRNA in vitro and in vivo
文献类型：期刊论文
| 作者 | Song Chun-Xia3,4; Niu Rong-Li1; Du Chang-Qine2; Yang Shao-Li1; Lin Xiu-Kun1 |
| 刊名 | PROGRESS IN BIOCHEMISTRY AND BIOPHYSICS
 |
| 出版日期 | 2007-12-01 |
| 卷号 | 34期号:12页码:1321-1326 |
| 关键词 | Zebrafish Thymidylate Synthase Electrophoretic Mobility Shift Assay (Emsa) Protein-rna Interaction Immunoprecipitation : Rt-pcr |
| ISSN号 | 1000-3282 |
| 文献子类 | Article |
| 英文摘要 | Thymidylate synthase (TS), an essential enzyme for DNA de novo synthesis, is a critical therapeutic target in cancer therapy. Previous study has shown that TS was able to bind to its own mRNA in human and E.coli, resulting in translational repression. Zebrafish is the best animal model for vertebrate study. In order to study the regulatory mechanism of zebrafish TS, the enzyme were expressed in E. coli BL21 (DE3) and it was purified to homogeneity. Electrophoretic mobility shift assay (EMSA) was used to detect the interaction of zebrafish TS protein and its own TS transcript in vitro and the results showed that zebrafish TS could bound with its own mRNA specifically. Further study revealed that zebrafish TS was able to interact with its own mRNA in vivo using immunoprecipitation : RT-PCR technique. The results provide evidence that zebrafish may be developed as an useful model for studying the anti-metabolism agents.; Thymidylate synthase (TS), an essential enzyme for DNA de novo synthesis, is a critical therapeutic target in cancer therapy. Previous study has shown that TS was able to bind to its own mRNA in human and E.coli, resulting in translational repression. Zebrafish is the best animal model for vertebrate study. In order to study the regulatory mechanism of zebrafish TS, the enzyme were expressed in E. coli BL21 (DE3) and it was purified to homogeneity. Electrophoretic mobility shift assay (EMSA) was used to detect the interaction of zebrafish TS protein and its own TS transcript in vitro and the results showed that zebrafish TS could bound with its own mRNA specifically. Further study revealed that zebrafish TS was able to interact with its own mRNA in vivo using immunoprecipitation : RT-PCR technique. The results provide evidence that zebrafish may be developed as an useful model for studying the anti-metabolism agents. |
| 语种 | 英语 |
| WOS记录号 | WOS:000252221800014 |
| 公开日期 | 2010-12-30 |
| 源URL | [http://ir.qdio.ac.cn/handle/337002/6297]  |
| 专题 | 海洋研究所_实验海洋生物学重点实验室 |
| 作者单位 | 1.Chinese Acad Sci, Inst Oceanol, Key Lab Expt Marine Biol, Qingdao 266071, Peoples R China 2.Weifang Med Univ, Weifang 261042, Peoples R China 3.Shandong Univ, Coll Life Sci, Jinan 250100, Peoples R China 4.Shandong Univ, Marine Coll, Weihai 264209, Peoples R China |
| 推荐引用方式 GB/T 7714 | Song Chun-Xia,Niu Rong-Li,Du Chang-Qine,et al. Zebrafish thymidylate synthase binds to its own mRNA in vitro and in vivo[J]. PROGRESS IN BIOCHEMISTRY AND BIOPHYSICS,2007,34(12):1321-1326. |
| APA | Song Chun-Xia,Niu Rong-Li,Du Chang-Qine,Yang Shao-Li,&Lin Xiu-Kun.(2007).Zebrafish thymidylate synthase binds to its own mRNA in vitro and in vivo.PROGRESS IN BIOCHEMISTRY AND BIOPHYSICS,34(12),1321-1326. |
| MLA | Song Chun-Xia,et al."Zebrafish thymidylate synthase binds to its own mRNA in vitro and in vivo".PROGRESS IN BIOCHEMISTRY AND BIOPHYSICS 34.12(2007):1321-1326. |
入库方式： OAI收割
来源：海洋研究所
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