Structural Transformation of the Tandem Ubiquitin-Interacting Motifs in Ataxin-3 and Their Cooperative Interactions with Ubiquitin Chains
文献类型：期刊论文
| 作者 | Song, Ai-Xin2; Zhou, Chen-Jie2; Peng, Yu1; Gao, Xue-Chao2; Zhou, Zi-Ren2; Fu, Qing-Shan2; Hong, Jing1; Lin, Dong-Hai1; Hu, Hong-Yu2 |
| 刊名 | PLOS ONE
 |
| 出版日期 | 2010-10-07 |
| 卷号 | 5期号:10 |
| ISSN号 | 1932-6203 |
| DOI | 10.1371/journal.pone.0013202 |
| 文献子类 | Article |
| 英文摘要 | The ubiquitin-interacting motif (UIM) is a short peptide with dual function of binding ubiquitin (Ub) and promoting ubiquitination. We elucidated the structures and dynamics of the tandem UIMs of ataxin-3 (AT3-UIM12) both in free and Ub-bound forms. The solution structure of free AT3-UIM12 consists of two alpha-helices and a flexible linker, whereas that of the Ub-bound form is much more compact with hydrophobic contacts between the two helices. NMR dynamics indicates that the flexible linker becomes rigid when AT3-UIM12 binds with Ub. Isothermal titration calorimetry and NMR titration demonstrate that AT3-UIM12 binds diUb with two distinct affinities, and the linker plays a critical role in association of the two helices in diUb binding. These results provide an implication that the tandem UIM12 interacts with Ub or diUb in a cooperative manner through an allosteric effect and dynamics change of the linker region, which might be related to its recognitions with various Ub chains and ubiquitinated substrates. |
| WOS关键词 | POLYGLUTAMINE DISEASE PROTEIN ; DEUBIQUITINATING ENZYME ATAXIN-3 ; MACHADO-JOSEPH-DISEASE ; NMR SOLUTION STRUCTURE ; BINDING DOMAINS ; CRYSTAL-STRUCTURE ; CHEMICAL-SHIFT ; RECOGNITION ; SYSTEM ; PROTEASOME |
| 资助项目 | National Natural Science Foundation of China[30600103] ; National Natural Science Foundation of China[30670431] ; National Natural Science Foundation of China[30870485] ; Shanghai Institutes for Biological Sciences[2008KIP201] ; National Basic Research Program of China[2006CB806508] ; National Basic Research Program of China[2006CB910305] ; National Basic Research Program of China[2007CB914304] |
| WOS研究方向 | Science & Technology - Other Topics |
| 语种 | 英语 |
| 出版者 | PUBLIC LIBRARY SCIENCE |
| WOS记录号 | WOS:000282633700009 |
| 源URL | [http://119.78.100.183/handle/2S10ELR8/278750]  |
| 专题 | 分析化学研究室 |
| 通讯作者 | Song, Ai-Xin |
| 作者单位 | 1.Chinese Acad Sci, Shanghai Inst Mat Med, Shanghai Inst Biol Sci, Shanghai 200031, Peoples R China 2.Chinese Acad Sci, State Key Lab Mol Biol, Inst Biochem & Cell Biol, Shanghai Inst Biol Sci, Shanghai, Peoples R China; |
| 推荐引用方式 GB/T 7714 | Song, Ai-Xin,Zhou, Chen-Jie,Peng, Yu,et al. Structural Transformation of the Tandem Ubiquitin-Interacting Motifs in Ataxin-3 and Their Cooperative Interactions with Ubiquitin Chains[J]. PLOS ONE,2010,5(10). |
| APA | Song, Ai-Xin.,Zhou, Chen-Jie.,Peng, Yu.,Gao, Xue-Chao.,Zhou, Zi-Ren.,...&Hu, Hong-Yu.(2010).Structural Transformation of the Tandem Ubiquitin-Interacting Motifs in Ataxin-3 and Their Cooperative Interactions with Ubiquitin Chains.PLOS ONE,5(10). |
| MLA | Song, Ai-Xin,et al."Structural Transformation of the Tandem Ubiquitin-Interacting Motifs in Ataxin-3 and Their Cooperative Interactions with Ubiquitin Chains".PLOS ONE 5.10(2010). |
入库方式： OAI收割
来源：上海药物研究所
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