引用本文: | 刘雪飞,范磊,王楠,黄新河.寿命调控同源蛋白Sch9与S6K1的结构与功能分析[J].生物信息学,2018,16(3):148-155. |
| LIU Xuefei,FAN Lei,WANG Nan,HUANG Xinhe.Structure and function analysis of lifespan regulation homologous protein Sch9 and S6K1[J].Chinese Journal of Bioinformatics,2018,16(3):148-155. |
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摘要: |
芽殖酵母Sch9与哺乳动物S6K1是保守的寿命调控同源蛋白,利用生物信息学手段比较分析了Sch9与S6K1的理化性质、亚细胞定位、信号肽和跨膜区、空间结构、蛋白质相互作用网络、序列同源性及进化关系,以期对Sch9与S6K1的结构功能的深入研究提供线索和基础。结果表明Sch9为酸性稳定性亲水蛋白,而S6K1为酸性不稳定的亲水蛋白,均无信号肽和跨膜区域,两者定位于细胞核的可能性最大。Sch9与S6K1的主要二级结构均为无规卷曲,在进化上相当保守,Sch9属于C2超家族和PKc_like超家族,S6K1属于PKc_like超家族。Sch9相互作用蛋白主要有Cyr1、Tor1、Tor2、Pkh1/2,而S6K1相互作用蛋白主要有PIK3CA、RHEB、Rps6、RPTOR、mTOR,显示两者的相互作用蛋白保守性也较强。同时,分析显示Sch9与S6K1均具有利于蛋白间相互作用的结构特点,为进一步深入研究Sch9与S6K1的分子功能及调控机制提供了一定的理论参考。 |
关键词: Sch9 S6K1 生物信息学 结构 功能 相互作用 |
DOI:10.12113/j.issn.1672-5565.201801005 |
分类号:Q255 |
文献标识码:A |
基金项目:四川省科技厅应用基础研究项目(No.2016JY0113);中国大学生科研训练计划项目(No.201710613066). |
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Structure and function analysis of lifespan regulation homologous protein Sch9 and S6K1 |
LIU Xuefei, FAN Lei, WANG Nan, HUANG Xinhe
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(School of Life Science and Engineering, Southwest Jiaotong University, Chengdu 610031, China)
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Abstract: |
Budding yeast Sch9 and mammalian S6K1 are important lifespan regulation homologous proteins. Bioinformatics methods were employed to analyze the chemical properties, subcellular localization, signal peptide, trans-membrane region, space structure, protein interaction networks, and hereditary conservation of Sch9 and S6K1, so as to provide clues and basis for further studying structure and function of these two proteins. Results showed that Sch9 was an acidic stable hydrophilic protein, while S6K1 was an acid labile hydrophilic protein. Both of them had no signal peptide and transmembrane regions, and both proteins were most likely located in the nucleus. The main secondary structures of Sch9 and S6K1 are random coil, both are quite conservative in evolution. Sch9 belongs to C2 superfamily and PKc_like superfamily, while S6K1 belongs to PKc_like superfamily. The interacting proteins of Sch9 include Cyr1, Tor1, Tor2, Pkh1/2. The interacting proteins of S6K1 are mainly PIK3CA, RHEB, Rps6, RPTOR, and Mtor. These findings indicate the interacting proteins of Sch9 and S6K1 are also conservative. Meanwhile,the analysis showed that both Sch9 and S6K1 had the structural features conducive to protein-protein interactions. This study provides some theoretical references for further research on molecular functions and regulatory mechanisms of Sch9 and S6K1. |
Key words: Sch9 S6K1 Bioinformatics Structure Function Interactive proteins |