Split mCherry as a new red bimolecular fluorescence complementation system for visualizing protein-protein interactions in living cells

@article{citeulike:2234344, abstract = {Bimolecular fluorescence complementation (BiFC) is a recently developed technique for detection of protein-protein interactions in living cells. In this study, a new red BiFC system was developed by splitting mCherry, a mutant monomeric red fluorescent protein, into two fragments between amino acids 159-160 and was verified using a pair of interacting proteins, SV40 large T antigen (LTag), and human p53 protein. By combined use of the mCherry-based red BiFC system with a Venus-based yellow BiFC system, the interaction between LTag and p53 as well as the interaction between sp100 and promyelocytic leukemia protein (PML), were detected simultaneously in Vero cells. The brilliant redness, short maturation time, and the long excitation and emission wavelengths (587/610 nm) of mCherry make the new BiFC system an excellent candidate for analyzing protein-protein interactions in living cells and for studying multiple protein-protein interactions when coupled with other BiFC systems.}, author = {Fan, Jin-Yu and Cui, Zong-Qiang and Wei, Hong-Ping and Zhang, Zhi-Ping and Zhou, Ya-Feng and Wang, Yun-Peng and Zhang, Xian-En }, citeulike-article-id = {2234344}, doi = {10.1016/j.bbrc.2007.12.101}, journal = {Biochemical and Biophysical Research Communications}, keywords = {bifc, fluorescent\_proteins, microscopy, technique}, month = {February}, number = {1}, pages = {47--53}, posted-at = {2008-03-21 14:37:53}, priority = {0}, title = {Split mCherry as a new red bimolecular fluorescence complementation system for visualizing protein-protein interactions in living cells}, url = {http://dx.doi.org/10.1016/j.bbrc.2007.12.101}, volume = {367}, year = {2008} }

TY - JOUR ID - citeulike:2234344 L3 - citeulike-article-id:2234344 TI - Split mCherry as a new red bimolecular fluorescence complementation system for visualizing protein-protein interactions in living cells JF - Biochemical and Biophysical Research Communications VL - 367 IS - 1 SP - 47 EP - 53 N2 - Bimolecular fluorescence complementation (BiFC) is a recently developed technique for detection of protein-protein interactions in living cells. In this study, a new red BiFC system was developed by splitting mCherry, a mutant monomeric red fluorescent protein, into two fragments between amino acids 159-160 and was verified using a pair of interacting proteins, SV40 large T antigen (LTag), and human p53 protein. By combined use of the mCherry-based red BiFC system with a Venus-based yellow BiFC system, the interaction between LTag and p53 as well as the interaction between sp100 and promyelocytic leukemia protein (PML), were detected simultaneously in Vero cells. The brilliant redness, short maturation time, and the long excitation and emission wavelengths (587/610 nm) of mCherry make the new BiFC system an excellent candidate for analyzing protein-protein interactions in living cells and for studying multiple protein-protein interactions when coupled with other BiFC systems. KW - bifc KW - fluorescent_proteins KW - microscopy KW - technique AU - Fan, Jin-Yu AU - Cui, Zong-Qiang AU - Wei, Hong-Ping AU - Zhang, Zhi-Ping AU - Zhou, Ya-Feng AU - Wang, Yun-Peng AU - Zhang, Xian-En PY - 2008/02/29/ UR - http://dx.doi.org/10.1016/j.bbrc.2007.12.101 ER -