Application of intra-molecular fluorescence complementation in the topology examination of polytopic proteins in living cells  

作　　者：Xingya Chang 

机构地区：[1]State Key Laboratory of Cognitive Neuroscience and Learning & IDG/McGovern Institute for Brain Research, College of Life Sciences, Beijing Normal University, Beijing 100875, China [2]Key Laboratory of Cell Proliferation and Regulation Biology, Ministry of Education, College of Life Science, Beijing Normal University, Beijing 100875, China [3]Center for Collaboration and Innovation in Brain and Learning Sciences, Beijing Normal University, Beijing 100875, China

出　　处：《Acta Biochimica et Biophysica Sinica》2015年第8期654-656,共3页生物化学与生物物理学报（英文版）

摘　　要：Bimolecular fluorescence complementation （BiFC） assay has been proved to be a very useful technique for detecting protein-protein, protein-DNA/RNA, and protein-ligand interactions under physio- logical or near-physiological conditions [1]. The basic strategy of BiFC is to split a fluorescent protein into two non-fluorescent frag- ments and fuse them to two proteins. When the interactions between these two proteins bring the split fragments into close proximity, the fluorescent protein is reconstituted. Thus, the fluorescence signals can reflect the interactions of the proteins. Here, instead of studying the in- teractions between two molecules, we report a novel, intra-molecular application of fluorescence complementation assay in studying the topology of proteins with multi-transmembrane domains （TMDs） in living cells.Bimolecular fluorescence complementation （BiFC） assay has been proved to be a very useful technique for detecting protein-protein, protein-DNA/RNA, and protein-ligand interactions under physio- logical or near-physiological conditions [1]. The basic strategy of BiFC is to split a fluorescent protein into two non-fluorescent frag- ments and fuse them to two proteins. When the interactions between these two proteins bring the split fragments into close proximity, the fluorescent protein is reconstituted. Thus, the fluorescence signals can reflect the interactions of the proteins. Here, instead of studying the in- teractions between two molecules, we report a novel, intra-molecular application of fluorescence complementation assay in studying the topology of proteins with multi-transmembrane domains （TMDs） in living cells.

分 类 号：Q51[生物学—生物化学] O438[机械工程—光学工程]