Open AccessInteraction between Bax and Bcl-XL proteins confirmed by partial acceptor photobleaching-based FRET imaging
Author(s) -
Fangfang Yang,
Mingde Du,
Xiaoping Wang,
Tongsheng Chen
Publication year - 2020
Publication title -
journal of innovative optical health sciences/journal of innovation in optical health science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.421
H-Index - 24
eISSN - 1793-5458
pISSN - 1793-7205
DOI - 10.1142/s179354582050011x
Subject(s) - förster resonance energy transfer , photobleaching , cytosol , fluorescence recovery after photobleaching , green fluorescent protein , fluorescence , mitochondrion , fluorescence lifetime imaging microscopy , fluorescence microscope , biophysics , acceptor , yellow fluorescent protein , live cell imaging , chemistry , biology , microbiology and biotechnology , physics , biochemistry , enzyme , optics , condensed matter physics , cell , gene
Exact interaction mechanism between Bax and Bcl-XL, two key Bcl-2 family proteins, is an interesting and controversial issue. Partial acceptor photobleaching-based quantitative fluorescence resonance energy transfer (FRET) measurement, PbFRET, is a widely used FRET quantification method in living cells. In this report, we implemented pixel-to-pixel PbFRET imaging on a wide-field microscope to map the FRET efficiency ([Formula: see text] images of single living HepG2 cells co-expressing CFP-Bax and YFP-Bcl-XL. The [Formula: see text] value between CFP-Bax and YFP-Bcl-XL was 4.59% in cytosol and 11.31% on mitochondria, conclusively indicating the direct interaction of the two proteins, and the interaction of the two proteins was strong on mitochondria and modest in cytosol.