生物谷报道：在科技部蛋白质组学攻关项目的支持下，陶涛教授课题组通过三年的潜心研究，运用先进的分子生物学，细胞生物学和蛋白质组学等手段，系统和全面的研究了人类蛋白水解小体亚基间相互作用，基于这些结果，陶涛教授课题组绘制了这些亚基间的相互作用图谱。该成果发表在最新一期的权威杂志《蛋白质组学》（Proteomics）上。
据悉，蛋白水解小体（proteasome）是细胞中调节蛋白质降解最重要的细胞器，具有调控基因表达，细胞分化，细胞凋亡和信号转导等重要的生理功能， 与肿瘤、老年痴呆等多种疾病的发生相关。蛋白水解小体是细胞中结构最复杂的蛋白质复合体，由近100个亚基蛋白质组成， 这些亚基在动态细胞中形成结构不一的蛋白水解小体复合物。 由于功能上的重要性和组成的复杂性，精确解析蛋白水解小体的结构，成为当今生物学领域的研究热点。获得蛋白质-蛋白质之间相互作用的信息是研究蛋白质结构和功能，了解细胞和机体生理奥秘最重要的一环。虽然人类已对低等生物（如细菌，酵母及果蝇）的蛋白水解小体亚基间相互作用进行了研究，但人类自身蛋白水解小体亚基间相互作用的系统研究还未见报道。这项研究为今后更加深入研究人类蛋白水解小体的结构和功能奠定了重要的基础。
该项研究得到了厦门市中山医院，军事医学科学院，国家南方基因中心和复旦大学等单位的大力协作。（来源：厦门大学）
生物谷推荐原始出处：
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 (taotao@xmu.edu.cn)
*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.
