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Zebrafish thymidylate synthase binds to its own mRNA in vitro and in vivo
Song Chun-Xia3,4; Niu Rong-Li1; Du Chang-Qine2; Yang Shao-Li1; Lin Xiu-Kun1
2007-12-01
发表期刊PROGRESS IN BIOCHEMISTRY AND BIOPHYSICS
ISSN1000-3282
卷号34期号:12页码:1321-1326
文章类型Article
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.
关键词Zebrafish Thymidylate Synthase Electrophoretic Mobility Shift Assay (Emsa) Protein-rna Interaction Immunoprecipitation : Rt-pcr
收录类别SCI
语种英语
WOS记录号WOS:000252221800014
引用统计
文献类型期刊论文
条目标识符http://ir.qdio.ac.cn/handle/337002/6296
专题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
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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.
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