Peripheral-type benzodiazepine receptor (PBR) aggregation and absence of steroidogenic acute regulatory protein (StAR)/PBR association in the mitochondrial membrane as determined by bioluminescence resonance energy transfer (BRET)

2007 ◽  
Vol 104 (1-2) ◽  
pp. 61-67 ◽  
Author(s):  
Randy L. Bogan ◽  
Tracy L. Davis ◽  
Gordon D. Niswender
Keyword(s):  
Energy Transfer ◽  
Mitochondrial Membrane ◽  
Regulatory Protein ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Benzodiazepine Receptor ◽  
Steroidogenic Acute Regulatory Protein ◽  
Bioluminescence Resonance Energy Transfer ◽  
Peripheral Type ◽  
Steroidogenic Acute Regulatory

scholarly journals Steroidogenic Acute Regulatory Protein and Peripheral-Type Benzodiazepine Receptor Associate at the Mitochondrial Membrane

Endocrinology ◽  
2001 ◽  
Vol 142 (1) ◽  
pp. 502-505 ◽  
Author(s):  
Louisa A. West ◽  
Regina D. Horvat ◽  
Deborah A. Roess ◽  
B. George Barisas ◽  
Jennifer L. Juengel ◽  
...  
Keyword(s):  
Mitochondrial Membrane ◽  
Regulatory Protein ◽  
Benzodiazepine Receptor ◽  
Steroidogenic Acute Regulatory Protein ◽  
Peripheral Type ◽  
Steroidogenic Acute Regulatory

scholarly journals Peripheral-Type Benzodiazepine Receptor-Mediated Action of Steroidogenic Acute Regulatory Protein on Cholesterol Entry into Leydig Cell Mitochondria

2005 ◽  
Vol 19 (2) ◽  
pp. 540-554 ◽  
Author(s):  
Thierry Hauet ◽  
Zhi-Xing Yao ◽  
Himangshu S. Bose ◽  
Christopher T. Wall ◽  
Zeqiu Han ◽  
...  
Keyword(s):  
Regulatory Protein ◽  
Benzodiazepine Receptor ◽  
Steroidogenic Acute Regulatory Protein ◽  
Rate Determining Step ◽  
Human Choriogonadotropin ◽  
Leydig Tumor Cells ◽  
Peripheral Type ◽  
Steroidogenic Acute Regulatory ◽  
And Function

Abstract Hormone-induced steroid biosynthesis begins with the transfer of cholesterol from intracellular stores into mitochondria. Steroidogenic acute regulatory protein (StAR) and peripheral-type benzodiazepine receptor (PBR) have been implicated in this rate-determining step of steroidogenesis. MA-10 mouse Leydig tumor cells were treated with and without oligodeoxynucleotides (ODNs) antisense to PBR and StAR followed by treatment with saturating concentrations of human choriogonadotropin. Treatment with ODNs antisense but not missense for both proteins inhibited the respective protein expression and the ability of the cells to synthesize steroids in response to human choriogonadotropin. Treatment of the cells with either ODNs antisense to PBR or a transducible peptide antagonist to PBR resulted in inhibition of the accumulation of the mature mitochondrial 30-kDa StAR protein, suggesting that the presence of PBR is required for StAR import into mitochondria. Addition of in vitro transcribed/translated 37-kDa StAR or a fusion protein of Tom20 (translocase of outer membrane) and StAR (Tom/StAR) to mitochondria isolated from control cells increased pregnenolone formation. Mitochondria isolated from cells treated with ODNs antisense, but not missense, to PBR failed to form pregnenolone and respond to either StAR or Tom/StAR proteins. Reincorporation of in vitro transcribed/translated PBR, but not PBR missing the cholesterol-binding domain, into MA-10 mitochondria rescued the ability of the mitochondria to form steroids and the ability of the mitochondria to respond to StAR and Tom/StAR proteins. These data suggest that both StAR and PBR proteins are indispensable elements of the steroidogenic machinery and function in a coordinated manner to transfer cholesterol into mitochondria.

scholarly journals Enhanced brightness of bacterial luciferase by bioluminescence resonance energy transfer

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Tomomi Kaku ◽  
Kazunori Sugiura ◽  
Tetsuyuki Entani ◽  
Kenji Osabe ◽  
Takeharu Nagai
Keyword(s):  
Energy Transfer ◽  
Mammalian Cells ◽  
Fluorescent Protein ◽  
Color Change ◽  
Yellow Fluorescent Protein ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Bioluminescence Resonance Energy Transfer ◽  
Bacterial Luciferase ◽  
Bacterial Bioluminescence

AbstractUsing the lux operon (luxCDABE) of bacterial bioluminescence system as an autonomous luminous reporter has been demonstrated in bacteria, plant and mammalian cells. However, applications of bacterial bioluminescence-based imaging have been limited because of its low brightness. Here, we engineered the bacterial luciferase (heterodimer of luxA and luxB) by fusion with Venus, a bright variant of yellow fluorescent protein, to induce bioluminescence resonance energy transfer (BRET). By using decanal as an externally added substrate, color change and ten-times enhancement of brightness was achieved in Escherichia coli when circularly permuted Venus was fused to the C-terminus of luxB. Expression of the Venus-fused luciferase in human embryonic kidney cell lines (HEK293T) or in Nicotiana benthamiana leaves together with the substrate biosynthesis-related genes (luxC, luxD and luxE) enhanced the autonomous bioluminescence. We believe the improved luciferase will forge the way towards the potential development of autobioluminescent reporter system allowing spatiotemporal imaging in live cells.

scholarly journals Greatly enhanced detection of a volatile ligand at femtomolar levels using bioluminescence resonance energy transfer (BRET)

2011 ◽  
Vol 29 (1) ◽  
pp. 119-124 ◽  
Author(s):  
Helen Dacres ◽  
Jian Wang ◽  
Virginia Leitch ◽  
Irene Horne ◽  
Alisha R. Anderson ◽  
...  
Keyword(s):  
Energy Transfer ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Bioluminescence Resonance Energy Transfer
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