生物谷報(bào)道：在科技部蛋白質(zhì)組學(xué)攻關(guān)項(xiàng)目的支持下,，陶濤教授課題組通過三年的潛心研究,，運(yùn)用先進(jìn)的分子生物學(xué),，細(xì)胞生物學(xué)和蛋白質(zhì)組學(xué)等手段,，系統(tǒng)和全面的研究了人類蛋白水解小體亞基間相互作用,，基于這些結(jié)果,，陶濤教授課題組繪制了這些亞基間的相互作用圖譜,。該成果發(fā)表在最新一期的權(quán)威雜志《蛋白質(zhì)組學(xué)》（Proteomics）上。
據(jù)悉,，蛋白水解小體（proteasome）是細(xì)胞中調(diào)節(jié)蛋白質(zhì)降解最重要的細(xì)胞器,，具有調(diào)控基因表達(dá)，細(xì)胞分化,，細(xì)胞凋亡和信號(hào)轉(zhuǎn)導(dǎo)等重要的生理功能,， 與腫瘤、老年癡呆等多種疾病的發(fā)生相關(guān),。蛋白水解小體是細(xì)胞中結(jié)構(gòu)最復(fù)雜的蛋白質(zhì)復(fù)合體,，由近100個(gè)亞基蛋白質(zhì)組成， 這些亞基在動(dòng)態(tài)細(xì)胞中形成結(jié)構(gòu)不一的蛋白水解小體復(fù)合物,。 由于功能上的重要性和組成的復(fù)雜性,，精確解析蛋白水解小體的結(jié)構(gòu)，成為當(dāng)今生物學(xué)領(lǐng)域的研究熱點(diǎn),。獲得蛋白質(zhì)-蛋白質(zhì)之間相互作用的信息是研究蛋白質(zhì)結(jié)構(gòu)和功能,，了解細(xì)胞和機(jī)體生理奧秘最重要的一環(huán)。雖然人類已對(duì)低等生物（如細(xì)菌,，酵母及果蠅）的蛋白水解小體亞基間相互作用進(jìn)行了研究,，但人類自身蛋白水解小體亞基間相互作用的系統(tǒng)研究還未見報(bào)道。這項(xiàng)研究為今后更加深入研究人類蛋白水解小體的結(jié)構(gòu)和功能奠定了重要的基礎(chǔ),。
該項(xiàng)研究得到了廈門市中山醫(yī)院,，軍事醫(yī)學(xué)科學(xué)院，國家南方基因中心和復(fù)旦大學(xué)等單位的大力協(xié)作,。（來源：廈門大學(xué)）
生物谷推薦原始出處：
Proteomics
Published Online: 9 Jan 2008
Cell Biology
Subunit-subunit interactions in the human 26S proteasome
Chuan Chen 1, Caoxin Huang 1, Shouhui Chen 2, Jie Liang 1, Wenbo Lin 1, Guifen Ke 1, Hongxin Zhang 1, Bing Wang 3, Jian Huang 4, Zeguang Han 4, Lixin Ma 5, Keke Huo 6, Xiaoming Yang 7, Pengyuan Yang 6, Fuchu He 7, Tao Tao, Dr. 1 2 *
1Key Laboratory for Cell Biology and Tumor Cell Engineering, the Ministry of Education, School of Life Sciences, Xiamen University, Xiamen, China
2Zhongshan Hospital of Xiamen, Xiamen, China
3Medical School of Xiamen, Xiamen, China
4National Center for Genomics, Shanghai, China
5Hubei University, Wuhan, China
6Fudan University, Shanghai, China
7Beijing Proteomics Center, Beijing, China
email: Tao Tao ([email protected])
*Correspondence to Tao Tao, School of Life Sciences, Xiamen University, Xiamen City, Fujian 361005, People's Republic of China Fax: +86-592-2182880
These authors contributed equally to this work.
Funded by:
Ministry of Science and Technology, China; Grant Number: 2004BA711A19-07
National Natural Science Foundation of China; Grant Number: 3047085, 90608007Y
Natural Science Foundation of Fujian Province; Grant Number: C0510003
Ministry of Education of China; Grant Number: 2005-383
Xiamen University; Grant Number: XK0014
Keywords
26S Proteasome ?Interaction ?Subunit ?Yeast two-hybrid analysis
Abstract
Ubiquitin-dependent proteolysis is mediated by the proteasome. To understand the structure and function of the human 26S proteasome, we cloned complete ORFs of 32 human proteasome subunits and conducted a yeast two-hybrid analysis of their interactions with each other. We observed that there are 114 interacting-pairs in the human 26S proteasome. About 10% (11/114) of these interacting-pairs was confirmed by the GST-pull down analysis. Among these observed interacting subunits, 58% (66/114) are novel and the rest 42% (48/114) has been reported previously in human or in other species. We observed new interactions between the 19S regulatory particle and the -rings of the 20S catalytic particle and therefore proposed a modified model of the 26S proteasome.
