9月2日,国际著名期刊Nature在线发表了加拿大多伦多大学等研究人员的一篇题为Interaction landscape of membrane-protein complexes in Saccharomyces cerevisiae的研究论文,文章首次描绘了膜蛋白相互作用组的全局拓扑图。
膜蛋白(membrane proteins ,MPs)复合体在各种各样的疾病中扮演着至关重要的角色,是主要的药物靶点。遗憾的是,目前对模式生物体内膜蛋白复合体的整体情况还没有系统的描述。
研究人员在没有变性去垢剂存在的条件下亲和纯化了1590个酿酒酵母的脂锚定膜蛋白复合体。这些共纯化蛋白首先采用串联质谱的方法进行鉴定,随后用于绘制高可信度的膜蛋白相互作用物理图,其中包括1726对与各种细胞膜系统联系的相互作用膜蛋白复合体和501个公认的杂聚肽复合体 。
这些研究揭示了真核生物膜生物学潜在的物理联系,描绘了膜蛋白相互作用组的全局拓扑图。(生物谷Bioon.com)
doi:10.1038/nature11354
PMC:
PMID:
Interaction landscape of membrane-protein complexes in Saccharomyces cerevisiae
Mohan Babu,James Vlasblom,Shuye Pu,Xinghua Guo,Chris Graham,Bj?rn D. M. Bean,Helen E. Burston,Franco J. Vizeacoumar,Jamie Snider,Sadhna Phanse, Vincent Fong,Yuen Yi C. Tam, Michael Davey,Olha Hnatshak,Navgeet Bajaj, Shamanta Chandran,Thanuja Punna,Constantine Christopolous,Victoria Wong, Analyn Yu,Gouqing Zhong,Joyce Li,Igor Stagljar, Elizabeth Conibear,Shoshana J. Wodak et al.
Macromolecular assemblies involving membrane proteins (MPs) serve vital biological roles and are prime drug targets in a variety of diseases1. Large-scale affinity purification studies of soluble-protein complexes have been accomplished for diverse model organisms, but no global characterization of MP-complex membership has been described so far. Here we report a complete survey of 1,590 putative integral, peripheral and lipid-anchored MPs from Saccharomyces cerevisiae, which were affinity purified in the presence of non-denaturing detergents. The identities of the co-purifying proteins were determined by tandem mass spectrometry and subsequently used to derive a high-confidence physical interaction map encompassing 1,726 membrane protein-protein interactions and 501 putative heteromeric complexes associated with the various cellular membrane systems. Our analysis reveals unexpected physical associations underlying the membrane biology of eukaryotes and delineates the global topological landscape of the membrane interactome..