Rhodopsin in reconstituted phospholipid vesicles. 1. Structural parameters and light-induced conformational changes detected by resonance energy transfer and quenching

Biochemistry ◽  
1983 ◽  
Vol 22 (1) ◽  
pp. 197-205 ◽  
Author(s):  
Hamutal Borochov-Neori ◽  
Mauricio Montal
Keyword(s):  
Energy Transfer ◽  
Conformational Changes ◽  
Structural Parameters ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Phospholipid Vesicles

Structural rearrangements of the motor protein prestin revealed by fluorescence resonance energy transfer

2009 ◽  
Vol 297 (2) ◽  
pp. C290-C298 ◽  
Author(s):  
Kristin Rule Gleitsman ◽  
Michihiro Tateyama ◽  
Yoshihiro Kubo
Keyword(s):  
Energy Transfer ◽  
Membrane Potential ◽  
Fluorescence Resonance Energy Transfer ◽  
Conformational Changes ◽  
Resonance Energy Transfer ◽  
Motor Protein ◽  
Resonance Energy ◽  
Outer Hair Cells ◽  
Nonlinear Capacitance ◽  
Fluorescence Resonance

Prestin is a membrane protein expressed in the outer hair cells (OHCs) in the cochlea that is essential for hearing. This unique motor protein transduces a change in membrane potential into a considerable mechanical force, which leads to a cell length change in the OHC. The nonlinear capacitance in cells expressing prestin is recognized to reflect the voltage-dependent conformational change of prestin, of which its precise nature remains unknown. In the present work, we aimed to detect the conformational changes of prestin by a fluorescence resonance energy transfer (FRET)-based technique. We heterologously expressed prestin labeled with fluorophores at the COOH- or NH2-terminus in human embryonic kidney-293T cells, and monitored FRET changes on depolarization-inducing high KCl application. We detected a significant decrease in intersubunit FRET both between the COOH-termini and between the COOH- and NH2-termini. A similar FRET decrease was observed when membrane potential was directly and precisely controlled by simultaneous patch clamp. Changes in FRET were suppressed by either of two treatments known to abolish nonlinear capacitance, V499G/Y501H mutation and sodium salicylate. Our results are consistent with significant movements in the COOH-terminal domain of prestin upon change in membrane potential, providing the first dynamic information on its molecular rearrangements.

Fluorescent resonance energy transfer -based biosensor for detecting conformational changes of Pin1

2018 ◽  
Vol 505 (2) ◽  
pp. 399-404 ◽  
Author(s):  
Masafumi Hidaka ◽  
Emiko Okabe ◽  
Kodai Hatakeyama ◽  
Heather Zook ◽  
Chiyoko Uchida ◽  
...  
Keyword(s):  
Energy Transfer ◽  
Conformational Changes ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Fluorescent Resonance Energy Transfer

scholarly journals Dibucaine interaction with phospholipid vesicles. A resonance energy-transfer study

1990 ◽  
Vol 189 (2) ◽  
pp. 387-393 ◽  
Author(s):  
Ana COUTINHO ◽  
Julia COSTA ◽  
Joaquim L. FARIA ◽  
Mario N. BERBERAN-SANTOS ◽  
Manuel J. E. PRIETO
Keyword(s):  
Energy Transfer ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Phospholipid Vesicles ◽  
Transfer Study
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