Structure, phosphorylation and U2AF65 binding of the N-terminal domain of splicing factor 1 during 3'-splice site recognition
文献类型：期刊论文
| 作者 | Zhang, Yun1,2; Madl, Tobias1,2,3; Bagdiul, Ivona4; Kern, Thomas1,2; Kang, Hyun-Seo1,2; Zou, Peijian1,2,5; Maeusbacher, Nina6; Sieber, Stephan A.6; Kraemer, Angela4; Sattler, Michael1,2,5 |
| 刊名 | NUCLEIC ACIDS RESEARCH
 |
| 出版日期 | 2013 |
| 卷号 | 41期号:2页码:1343-1354 |
| 英文摘要 | Recognition of the 3'-splice site is a key step in pre-mRNA splicing and accomplished by a dynamic complex comprising splicing factor 1 (SF1) and the U2 snRNP auxiliary factor 65-kDa subunit (U2AF65). Both proteins mediate protein-protein and protein-RNA interactions for cooperative RNA-binding during spliceosome assembly. Here, we report the solution structure of a novel helix-hairpin domain in the N-terminal region of SF1 (SF1(NTD)). The nuclear magnetic resonance- and small-angle X-ray scattering-derived structure of a complex of the SF1(NTD) with the C-terminal U2AF homology motif domain of U2AF65 (U2AF65(UHM)) reveals that, in addition to the known U2AF65(UHM)-SF1 interaction, the helix-hairpin domain forms a secondary, hydrophobic interface with U2AF65(UHM), which locks the orientation of the two subunits. Mutational analysis shows that the helix hairpin is essential for cooperative formation of the ternary SF1-U2AF65-RNA complex. We further show that tandem serine phosphorylation of a conserved Ser80-Pro81-Ser82-Pro83 motif rigidifies a long unstructured linker in the SF1 helix hairpin. Phosphorylation does not significantly alter the overall conformations of SF1, SF1-U2AF65 or the SF1-U2AF65-RNA complexes, but slightly enhances RNA binding. Our results indicate that the helix-hairpin domain of SF1 is required for cooperative 3'-splice site recognition presumably by stabilizing a unique quaternary arrangement of the SF1-U2AF65-RNA complex. |
| WOS标题词 | Science & Technology ; Life Sciences & Biomedicine |
| 类目[WOS] | Biochemistry & Molecular Biology |
| 研究领域[WOS] | Biochemistry & Molecular Biology |
| 关键词[WOS] | POLYPYRIMIDINE TRACT RECOGNITION ; ANGLE SCATTERING DATA ; N-15 NMR RELAXATION ; FACTOR SF1 ; PROTEIN RECOGNITION ; RNA ; SPECTROSCOPY ; DYNAMICS ; MACROMOLECULES ; CONSERVATION |
| 收录类别 | SCI |
| 语种 | 英语 |
| WOS记录号 | WOS:000314121100060 |
| 公开日期 | 2015-01-22 |
| 源URL | [http://124.16.173.210/handle/311007/605]  |
| 专题 | 天津工业生物技术研究所_蛋白质工程实验室 邹培建_期刊论文 |
| 作者单位 | 1.Helmholtz Zentrum Munchen, Inst Struct Biol, D-85764 Neuherberg, Germany 2.Tech Univ Munich, Dept Chem, Munich Ctr Integrated Prot Sci, Chair Biomol NMR, D-85747 Garching, Germany 3.Karl Franzens Univ Graz, Dept Bioorgan Chem, Inst Chem, A-8010 Graz, Austria 4.Univ Geneva, Dept Cell Biol, Fac Sci, CH-1211 Geneva 4, Switzerland 5.Chinese Acad Sci, Tianjin Inst Ind Biotechnol, Tianjin 300308, Peoples R China 6.Tech Univ Munich, Dept Chem, Munich Ctr Integrated Prot Sci, Chair Organ Chem 2, D-85747 Garching, Germany |
| 推荐引用方式 GB/T 7714 | Zhang, Yun,Madl, Tobias,Bagdiul, Ivona,et al. Structure, phosphorylation and U2AF65 binding of the N-terminal domain of splicing factor 1 during 3'-splice site recognition[J]. NUCLEIC ACIDS RESEARCH,2013,41(2):1343-1354. |
| APA | Zhang, Yun.,Madl, Tobias.,Bagdiul, Ivona.,Kern, Thomas.,Kang, Hyun-Seo.,...&Sattler, Michael.(2013).Structure, phosphorylation and U2AF65 binding of the N-terminal domain of splicing factor 1 during 3'-splice site recognition.NUCLEIC ACIDS RESEARCH,41(2),1343-1354. |
| MLA | Zhang, Yun,et al."Structure, phosphorylation and U2AF65 binding of the N-terminal domain of splicing factor 1 during 3'-splice site recognition".NUCLEIC ACIDS RESEARCH 41.2(2013):1343-1354. |
入库方式： OAI收割
来源：天津工业生物技术研究所
浏览0
下载0
收藏0
其他版本
除非特别说明，本系统中所有内容都受版权保护，并保留所有权利。