Thu, 21 Aug 2008 14:42:33 BST CiteULike: lechristophe's Wei http://www.citeulike.org/user/lechristophe/author/Wei CiteULike.org en-gb Copyright © 2004-2008 citeulike.org http://www.citeulike.org/user/lechristophe/article/2234344 <i>Biochemical and Biophysical Research Communications, Vol. 367, No. 1. (29 February 2008), pp. 47-53.</i><br /><br />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. Split mCherry as a new red bimolecular fluorescence complementation system for visualizing protein-protein interactions in living cells Jin-Yu Fan Zong-Qiang Cui Hong-Ping Wei Zhi-Ping Zhang Ya-Feng Zhou Yun-Peng Wang Xian-En Zhang doi:10.1016/j.bbrc.2007.12.101 Biochemical and Biophysical Research Communications, Vol. 367, No. 1. (29 February 2008), pp. 47-53. 2008-01-15T09:48:13-00:00 2008 Biochemical and Biophysical Research Communications 367 1 47 53 bifc fluorescent_proteins microscopy technique